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Artículos de revistas sobre el tema "Dissociation constant of inhibitor"

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Publicado: 4 de junio de 2021

Última modificación: 20 de febrero de 2023

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1

Björk, I., E. Pol, E. Raub-Segall, M. Abrahamson, A. D. Rowan, and J. S. Mort. "Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes." Biochemical Journal 299, no. 1 (April 1, 1994): 219–25. http://dx.doi.org/10.1042/bj2990219.

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The importance of the N-terminal region of human cystatin C or chicken cystatin for the kinetics of interactions of the inhibitors with four cysteine proteinases was characterized. The association rate constants for the binding of recombinant human cystatin C to papain, ficin, actinidin and recombinant rat cathepsin B were 1.1 x 10(7), 7.0 x 10(6), 2.4 x 10(6) and 1.4 x 10(6) M-1.s-1, whereas the corresponding dissociation rate constants were 1.3 x 10(-7), 9.2 x 10(-6), 4.6 x 10(-2) and 3.5 x 10(-4) s-1. N-Terminal truncation of the first ten residues of the inhibitor negligibly affected the a

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2

Hofsteenge, J., H. Taguchi, and S. R. Stone. "Effect of thrombomodulin on the kinetics of the interaction of thrombin with substrates and inhibitors." Biochemical Journal 237, no. 1 (July 1, 1986): 243–51. http://dx.doi.org/10.1042/bj2370243.

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Thrombomodulin decreased by 20-30% the Michaelis constant of two tripeptidyl p-nitroanilide substrates of thrombin. Thrombomodulin increased the rate of inactivation of thrombin by two peptidyl chloromethane inhibitors by a similar amount. This effect appeared to be due to a decrease in the dissociation constants of the inhibitors. An improved method for the separation of fibrinopeptides A and B by h.p.l.c. was developed, and this method was used to study the effect of thrombomodulin on the thrombin-catalysed cleavage of fibrinogen. In this reaction, thrombomodulin was a competitive inhibitor

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3

Boudier, C., and J. G. Bieth. "Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor." Biochemical Journal 303, no. 1 (October 1, 1994): 61–68. http://dx.doi.org/10.1042/bj3030061.

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N-chlorosuccinimide oxidizes one of the methionine residues of mucus proteinase inhibitor with a second-order rate constant of 1.5 M-1.s-1. Cyanogen bromide cleavage and NH2-terminal sequencing show that the modified residue is methionine-73, the P′1 component of the inhibitor's active centre. Oxidation of the inhibitor decreases its neutrophil elastase inhibitory capacity but does not fully abolish it. The kinetic parameters describing the elastase-oxidized inhibitor interaction are: association rate constant kass. = 2.6 x 10(5) M-1.s-1, dissociation rate constant kdiss. = 2.9 x 10(-3) s-1 an

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4

Brown, Nicholas G., Dar-Chone Chow, and Timothy Palzkill. "BLIP-II Is a Highly Potent Inhibitor of Klebsiella pneumoniae Carbapenemase (KPC-2)." Antimicrobial Agents and Chemotherapy 57, no. 7 (April 15, 2013): 3398–401. http://dx.doi.org/10.1128/aac.00215-13.

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ABSTRACTβ-Lactamase inhibitory protein II (BLIP-II) is a potent inhibitor of class A β-lactamases. KPC-2 is a class A β-lactamase that is capable of hydrolyzing carbapenems and has become a widespread source of resistance to these drugs for Gram-negative bacteria. Determination of association and dissociation rate constants for binding between BLIP-II and KPC-2 reveals a very tight interaction with a calculated (koff/kon) equilibrium dissociation constant of 76 fM (76 × 10−15M).

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5

LOHSE, Anders, Tore HARDLEI, Astrid JENSEN, Igor W. PLESNER та Mikael BOLS. "Investigation of the slow inhibition of almond β-glucosidase and yeast isomaltase by 1-azasugar inhibitors: evidence for the ‘direct binding’ model". Biochemical Journal 349, № 1 (26 червня 2000): 211–15. http://dx.doi.org/10.1042/bj3490211.

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(-)-1-Azafagomine [(3R,4R,5R)-4,5-dihydroxy-3-hydroxymethylhexahydropyridazine; inhibitor 1] is a potent glycosidase inhibitor designed to mimic the transition state of a substrate undergoing glycoside cleavage. The inhibition of glycosidases by inhbitor 1 and analogues has been found to be a relatively slow process. This ‘slow inhibition’ process was investigated in the inhibition of almond β-glucosidase and yeast isomaltase by inhibitor 1 and analogues. Progress-curve experiments established that the time-dependent inhibition of both enzymes by inhibitor 1 was a consequence of relatively slo

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6

Lindahl, P., E. Raub-Segall, S. T. Olson, and I. Björk. "Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations." Biochemical Journal 276, no. 2 (June 1, 1991): 387–94. http://dx.doi.org/10.1042/bj2760387.

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Papain was labelled by attachment of the fluorescent groups 2-(4′-acetamidoanilino)naphthalene-6-sulphonic acid (AANS) or N-(acetylaminoethyl)-8-naphthylamine-1-sulphonic acid (AEDANS) to the active-site cysteine residue, with the aim of using the labelled papains as probes in competitive titrations of unlabelled cysteine proteinases with their inhibitors. The interaction between the labelled papains and cystatins was accompanied by an increase in fluorescence emission of up to 38-fold for AANS-papain and approximately 3.5-fold for AEDANS-papain. Fluorescence titrations gave dissociation equil

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7

Lindhout, T., G. Willems, R. Blezer, and H. C. Hemker. "Kinetics of the inhibition of human factor Xa by full-length and truncated recombinant tissue factor pathway inhibitor." Biochemical Journal 297, no. 1 (January 1, 1994): 131–36. http://dx.doi.org/10.1042/bj2970131.

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The inhibition equilibrium and kinetics of association and dissociation of the binding of three types of recombinant tissue factor pathway inhibitor (TFPI), namely full-length TFPI, C-terminal-truncated TFPI, and TFPI without the third Kunitz domain (TFPI1-161), to factor Xa have been measured. Formation and dissociation of the complexes were monitored by continuous measurement of the changes in the rate of hydrolysis of a peptidyl-p-nitroanilide substrate. Progress curves of product formation were fitted to a set of equations describing a one-step bimolecular inhibitory reaction in the presen

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8

Ahmad, Suhail, R. K. Bhatnagar, and T. A. Venkitasubramanian. "Ornithine transcarbamylase from Mycobacterium smegmatis ATCC 14468: purification, properties, and reaction mechanism." Biochemistry and Cell Biology 64, no. 12 (December 1, 1986): 1349–55. http://dx.doi.org/10.1139/o86-177.

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Ornithine transcarbamylase (EC 2.1.3.3) has been purified 980-fold from Mycobacterium smegmatis and has a molecular weight of 116 000. Initial velocity determinations indicated that the reaction proceeds via a sequential kinetic mechanism. The limiting Michaelis constants for carbamyl phosphate (KmA) and ornithine (KmB) and the dissociation constant for carbamyl phospate (Kia) were found to be 0.20, 0.25, and 0.07 mM, respectively. Ornithine at higher concentrations acted as an uncompetitive inhibitor when carbamyl phosphate was the variable substrate. Phosphate was a competitive inhibitor wit

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9

Jin, Byung-Ju, Jay R. Thiagarajah, and A. S. Verkman. "Convective washout reduces the antidiarrheal efficacy of enterocyte surface–targeted antisecretory drugs." Journal of General Physiology 141, no. 2 (January 28, 2013): 261–72. http://dx.doi.org/10.1085/jgp.201210885.

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Secretory diarrheas such as cholera are a major cause of morbidity and mortality in developing countries. We previously introduced the concept of antisecretory therapy for diarrhea using chloride channel inhibitors targeting the cystic fibrosis transmembrane conductance regulator channel pore on the extracellular surface of enterocytes. However, a concern with this strategy is that rapid fluid secretion could cause convective drug washout that would limit the efficacy of extracellularly targeted inhibitors. Here, we developed a convection–diffusion model of washout in an anatomically accurate

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10

Bernal, A. López, S. Buckley, C. M. P. Rees, and J. M. Marshall. "Meclofenamate inhibits prostaglandin E binding and adenylyl cyclase activation in human myometrium." Journal of Endocrinology 129, no. 3 (June 1991): 439–45. http://dx.doi.org/10.1677/joe.0.1290439.

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ABSTRACT The effect of sodium meclofenamate on the binding of [3H]prostaglandin E2 ([3H]PGE2) to membranes from human myometrium was investigated. Meclofenamate inhibited the binding of [3H]PGE2 to high-affinity (dissociation constant 1·5 nmol/l) sites in a reversible dose-dependent manner (inhibition constant 11 μmol/l). The mechanism of inhibition was mainly competitive, but at high doses of meclofenamate (≥ 100 μmol/l) there was loss of PGE receptor sites. Of several PG synthesis inhibitors tested, only meclofenamate and, to a lesser extent, mefenamic acid had a significant inhibitory effec

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11

VENÄLÄINEN, Jarkko I., Risto O. JUVONEN, J. Arturo GARCIA-HORSMAN, Erik A. A. WALLÉN, Johannes A. M. CHRISTIAANS, Elina M. JARHO, Jukka GYNTHER, and Pekka T. MÄNNISTÖ. "Slow-binding inhibitors of prolyl oligopeptidase with different functional groups at the P1 site." Biochemical Journal 382, no. 3 (September 7, 2004): 1003–8. http://dx.doi.org/10.1042/bj20040992.

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POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. It has been noted that certain functional groups at the P1 site of the inhibitor, which correspond to the substrate residue on the N-terminal side of the bond to be cleaved, increase the inhibitory potency. However, detailed mechanistic and kinetic analysis of the inhibition has not been studied. In the present study, we examined the effect of different functional groups at the P1 s

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12

Levesque, Marc C., Dipak K. Ghosh, Bethany E. Beasley, Youwei Chen, Alicia D. Volkheimer, Charles W. O’Loughlin, Jon P. Gockerman, Joseph O. Moore, and J. Brice Weinberg. "Induction of Chronic Lymphocytic Leukemia (CLL) Apoptosis by Nitric Oxide Synthase (NOS) Inhibitors: Drug Efficacy Correlates with Lipid Solubility and NOS1 Dissociation Constant." Blood 106, no. 11 (November 16, 2005): 5044. http://dx.doi.org/10.1182/blood.v106.11.5044.5044.

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Abstract The viability of CLL cells may be dependent on the autocrine production of nitric oxide because nitric oxide synthase (NOS) inhibitors induce CLL cell apoptosis and CLL cells express inducible NOS (NOS2). Our previous study indicated that the non-specific NOS inhibitor NMMA induced CLL cell apoptosis but only at high concentrations (&gt; 1 mM) (Levesque et al., Leukemia17:442, 2003). Therefore, we performed the current study to identify NOS inhibitors that induce CLL cell apoptosis at lower concentrations and to understand factors that promote NOS inhibitor-induced CLL cell toxici

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13

Waley, S. G. "The kinetics of slow-binding and slow, tight-binding inhibition: the effects of substrate depletion." Biochemical Journal 294, no. 1 (August 15, 1993): 195–200. http://dx.doi.org/10.1042/bj2940195.

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Inhibitors with dissociation constants in the micromolar to nanomolar range are important, but hard to characterize kinetically, especially when the substrate concentration in the assay is less than Km. When inhibition increases during the course of the assay (slow-binding inhibition) the concentration of substrate may decrease appreciably. Methods that take substrate depletion into account are described for analysing experiments in which the initial substrate concentration is below Km. Fitting progress curves gives the rate constants for the second (slow) step in a two-step mechanism. An appr

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14

Mende, Katrin, Goetz Nowak, and Mercedes López. "Improvement of the specificity of dipetarudin by site directed mutagenesis." Thrombosis and Haemostasis 93, no. 03 (2005): 430–36. http://dx.doi.org/10.1160/th04-08-0480.

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SummaryProtease specificity is crucial to the design of thrombin inhibitors as inhibition of other physiologically relevant serine-proteases can compromise their clinical use. Dipetarudin, a potent thrombin inhibitor, also inhibits trypsin and plasmin. Due to the specificity of an inhibitor being influenced by the amino acid residue at the P1 position, we replaced the Arg10 at P1 position of dipetarudin by a histidine, which is the P1 residue of rhodniin, a very specific thrombin inhibitor. The amino acid replacement was carried out by site directed mutagenesis. The mutant, dipetarudin R10H, s

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15

Ramić, Alma, Ana Matošević, Barbara Debanić, Ana Mikelić, Ines Primožič, Anita Bosak, and Tomica Hrenar. "Synthesis, Biological Evaluation and Machine Learning Prediction Model for Fluorinated Cinchona Alkaloid-Based Derivatives as Cholinesterase Inhibitors." Pharmaceuticals 15, no. 10 (September 30, 2022): 1214. http://dx.doi.org/10.3390/ph15101214.

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A series of 46 Cinchona alkaloid derivatives that differ in positions of fluorine atom(s) in the molecule were synthesized and tested as human acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors. All tested compounds reversibly inhibited AChE and BChE in the nanomolar to micromolar range; for AChE, the determined enzyme-inhibitor dissociation constants (Ki) ranged from 3.9–80 µM, and 0.075–19 µM for BChE. The most potent AChE inhibitor was N-(para-fluorobenzyl)cinchoninium bromide, while N-(meta-fluorobenzyl)cinchonidinium bromide was the most potent BChE inhibitor with Ki

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16

Martin, G. E. M., N. G. Rutherford, P. J. F. Henderson, and A. R. Walmsley. "Kinetics and thermodynamics of the binding of forskolin to the galactose-H+ transport protein, GalP, of Escherichia coli." Biochemical Journal 308, no. 1 (May 15, 1995): 261–68. http://dx.doi.org/10.1042/bj3080261.

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The binding of the transport inhibitor, forskolin, to the galactose-H+ symporter, GalP, of Escherichia coli was evaluated by equilibrium and time-resolved fluorescence measurements. A quench in protein fluorescence of 8-12% was observed upon the binding of forskolin. The overall dissociation constant (Kd) for forskolin determined by fluorescence titration ranged between 1.2 and 2.2 microM, which is similar to that reported from equilibrium dialysis measurements of the binding of [3H]forskolin (Kd = 0.9-1.4 microM). The kinetics of forskolin binding were measured by stopped-flow fluorescence me

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17

Chen, C. K., T. J. McDonald, and E. E. Daniel. "Characterization of galanin receptor in canine small intestinal circular muscle synaptosomes." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 1 (January 1, 1994): G106—G112. http://dx.doi.org/10.1152/ajpgi.1994.266.1.g106.

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We used 125I-galanin (porcine) as ligand to study the galanin receptors in circular muscle and deep muscular plexus from canine small intestine. Specific binding sites were found in both nerve and muscle membranes. On synaptosomal membranes, the equilibrium binding study showed a high-affinity (dissociation constant, Kd = 1.1 +/- 0.13 nM; maximum binding capacity, Bmax = 244 +/- 2.1 fmol/mg) binding site. The specific binding of 125I-galanin to nerve membrane was inhibited by galanin or NH2-terminal galanin fragments but not by the COOH-terminal fragment. Computer analysis suggested a two-site

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18

Raines, Douglas E., and Vinu T. Zachariah. "Isoflurane Increases the Apparent Agonist Affinity of the Nicotinic Acetylcholine Receptor by Reducing the Microscopic Agonist Dissociation Constant." Anesthesiology 92, no. 3 (March 1, 2000): 775–85. http://dx.doi.org/10.1097/00000542-200003000-00021.

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Background Isoflurane increases the apparent agonist affinity of ligand-gated ion channels. This action reflects a reduction in the receptor's agonist dissociation constant and/or the preopen/open channel state equilibrium. To evaluate the effect of isoflurane on each of these kinetic constants in the nicotinic acetylcholine receptor, the authors analyzed isoflurane's actions on (1) the binding of the fluorescent agonist Dns-C6-Cho to the nicotinic acetylcholine receptor's agonist self-inhibition site and (2) the desensitization kinetics induced by the binding of the weak partial agonist suber

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19

FRANSSEN, Jo, Irene SALEMINK, George M. WILLEMS, Tze-Chein WUN, H. Coenraad HEMKER, and Theo LINDHOUT. "Prothrombinase is protected from inactivation by tissue factor pathway inhibitor: competition between prothrombin and inhibitor*." Biochemical Journal 323, no. 1 (April 1, 1997): 33–37. http://dx.doi.org/10.1042/bj3230033.

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The inhibition of prothrombinase by tissue factor pathway inhibitor (TFPI) has been studied in the presence and absence of prothrombin. The rate constant of association of prothrombinase with full-length TFPI was 2.1×107 M-1ċs-1 and 0.05×107 M-1ċs-1 for the reaction with C-terminus truncated TFPI (TFPI1-161). The rate constant of dissociation was 0.65×10-4 s-1 in both cases. The rate constant of inhibition of prothrombinase by TFPI1-161 was similar to that of solution-phase factor Xa. In contrast, phospholipids and factor Va enhanced the association rate of the reaction between factor Xa and f

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20

Zhu, Jingjing, Jeroen Declercq, Bart Roucourt, Gholamreza H. Ghassabeh, Sandra Meulemans, Jörg Kinne, Guido David, et al. "Generation and characterization of non-competitive furin-inhibiting nanobodies." Biochemical Journal 448, no. 1 (October 18, 2012): 73–82. http://dx.doi.org/10.1042/bj20120537.

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The PC (proprotein convertase) furin cleaves a large variety of proproteins and hence plays a major role in many pathologies. Therefore furin inhibition might be a good strategy for therapeutic intervention, and several furin inhibitors have been generated, although none are entirely furin-specific. To reduce potential side effects caused by cross-reactivity with other proteases, dromedary heavy-chain-derived nanobodies against catalytically active furin were developed as specific furin inhibitors. The nanobodies bound only to furin but not to other PCs. Upon overexpression in cell lines, they

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21

Stachyra, Thérèse, Marie-Claude Péchereau, Jean-Michel Bruneau, Monique Claudon, Jean-Marie Frère, Christine Miossec, Kenneth Coleman та Michael T. Black. "Mechanistic Studies of the Inactivation of TEM-1 and P99 by NXL104, a Novel Non-β-Lactam β-Lactamase Inhibitor". Antimicrobial Agents and Chemotherapy 54, № 12 (4 жовтня 2010): 5132–38. http://dx.doi.org/10.1128/aac.00568-10.

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ABSTRACT NXL104 is a potent inhibitor of class A and C serine β-lactamases, including KPC carbapenemases. Native and NXL104-inhibited TEM-1 and P99 β-lactamases analyzed by liquid chromatography-electrospray ionization-time of flight mass spectrometry revealed that the inactivated enzymes formed a covalent adduct with NXL104. The principal inhibitory characteristics of NXL104 against TEM-1 and P99 β-lactamases were determined, including partition ratios, dissociation constants (K), rate constants for deactivation (k 2), and reactivation rates. NXL104 is a potent inhibitor of TEM-1 and P99, cha

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22

López, Mercedes, Goetz Nowak, and Thomas Bitter. "Design and characterization of dipetacompinR10H, a dipetalogastin II-derived, classical competitive thrombin inhibitor." Thrombosis and Haemostasis 97, no. 01 (2007): 139–45. http://dx.doi.org/10.1160/th06-06-0308.

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SummaryThe design of small chimeric thrombin inhibitors based on the structure of dipetalogastin II has been previously described. These proteins are effective inhibitors of thrombin showing slow binding or slow, tight-binding kinetics. We report here about dipetacompinR10H, a new dipetalogastin II-derived chimeric thrombin inhibitor, which exhibits classical competitive kinetics. The dissociation constant Ki of dipetacompinR10H was determined to be 17.1 ± 0.8 pM. In various coagulation assays it showed a comparable anticoagulant activity like r-hirudin and r-dipetalogastin II. DipetacompinR10

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23

Blessinger, K. J., and G. Tunnicliff. "Kinetics of inactivation of 4-aminobutyrate aminotransferase by 3-bromopyruvate." Biochemistry and Cell Biology 70, no. 8 (August 1, 1992): 716–19. http://dx.doi.org/10.1139/o92-109.

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3-Bromopyruvate inhibited 4-aminobutyrate aminotransferase (EC 2.6.1.19) from Pseudomonas fluorescens, apparently irreversibly. Kinetics of this inactivation were studied by continuously monitoring the enzyme reaction at 30 °C in the presence of inhibitor. Irrespective of how high an inhibitor concentration was present, a maximum rate of inactivation was eventually achieved (5.9 × 10−3 s−1), indicating the formation of a reversible inhibitor–enzyme complex before the final inactivation step. The dissociation constant of this complex was found to be 6.5 μM. This affinity labelling by 3-bromopyr

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24

Dong, Qi, Na Hu, Huilan Yue та Honglun Wang. "Inhibitory Activity and Mechanism Investigation of Hypericin as a Novel α-Glucosidase Inhibitor". Molecules 26, № 15 (28 липня 2021): 4566. http://dx.doi.org/10.3390/molecules26154566.

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α-glucosidase is a major enzyme that is involved in starch digestion and type 2 diabetes mellitus. In this study, the inhibition of hypericin by α-glucosidase and its mechanism were firstly investigated using enzyme kinetics analysis, real-time interaction analysis between hypericin and α-glucosidase by surface plasmon resonance (SPR), and molecular docking simulation. The results showed that hypericin was a high potential reversible and competitive α-glucosidase inhibitor, with a maximum half inhibitory concentration (IC50) of 4.66 ± 0.27 mg/L. The binding affinities of hypericin with α-gluco

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25

Gadosy, Timothy A., та Oswald S. Tee. "Spectator catalysis in the cleavage of p-nitrophenyl acetate and p-nitrophenyl hexanoate by "hydroxypropyl-β-cyclodextrin"". Canadian Journal of Chemistry 74, № 5 (1 травня 1996): 745–52. http://dx.doi.org/10.1139/v96-081.

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Aliphatic alcohols that form host–guest complexes with "hydroxypropyl-β-cyclodextrin" retard the cleavage of m-nitrophenyl acetate by hydroxypropyl-β-cyclodextrin in basic aqueous solution, due to competitive inhibition. By contrast, these same species do not inhibit the reaction of p-nitrophenyl acetate and p-nitrophenyl hexanoate to the same extent and, in some cases, the addition of alcohols serves to increase the rate of reaction. The observed reaction kinetics require the presence of a process that has one molecule of the "potential inhibitor" in the transition state for ester cleavage. R

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26

Inglese, James, Richard A. Blatchly, and Stephen J. Benkovic. "A multisubstrate adduct inhibitor of a purine biosynthetic enzyme with a picomolar dissociation constant." Journal of Medicinal Chemistry 32, no. 5 (May 1989): 937–40. http://dx.doi.org/10.1021/jm00125a002.

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Yamanishi, R., J. Kotera, T. Fushiki, T. Soneda, T. Saitoh, T. Oomori, T. Satoh, and E. Sugimoto. "A specific binding of the cholecystokinin-releasing peptide (monitor peptide) to isolated rat small-intestinal cells." Biochemical Journal 291, no. 1 (April 1, 1993): 57–63. http://dx.doi.org/10.1042/bj2910057.

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A specific binding of the cholecystokinin (CCK)-releasing peptide (monitor peptide) to isolated rat jejunal mucosal cells was investigated. The 125I-labelled purified monitor peptide bound to the rat jejunal cells, and a large excess amount of the non-labelled monitor peptide inhibited the binding. The binding was completed within 60 min at 37 degrees C. The optimum pH for the binding was 8-9. A Scatchard plot of the specific binding was linear, and the dissociation constant was 50 nM. The density of the monitor-peptide-binding sites was high in duodenum but low in ileal and absent in colonic

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28

Liu, Yaqin, Yuanjiang Pan та Yuhong Xu. "Binding Investigation of Integrin αvβ3 With Its Inhibitors by SPR Technology and Molecular Docking Simulation". Journal of Biomolecular Screening 15, № 2 (19 січня 2010): 131–37. http://dx.doi.org/10.1177/1087057109356207.

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Integrins play critical roles in the process of angiogenesis and are attractive targets for anticancer therapies. It is desirable to develop new types of small-molecule inhibitors of integrin. Herein, the binding features of several inhibitors to integrin αvβ3 have been studied by surface plasmon resonance (SPR) biosensor technology and molecular docking analyses. The SPR results indicated that the equilibrium dissociation constant (KD) values are evaluated for the inhibitors and showed that the KD value of cyclopeptide c-Lys is much lower than the reference molecule. In addition, the 3D struc

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29

Mock, W. L., D. J. Freeman, and M. Aksamawati. "Fluxionate Lewis acidity of the Zn2+ ion in carboxypeptidase A." Biochemical Journal 289, no. 1 (January 1, 1993): 185–93. http://dx.doi.org/10.1042/bj2890185.

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Competitive inhibition constants Ki for a series of phenol-ring-substituted derivatives of alpha-(2-hydroxyphenyl)benzenepropanoic acid have been ascertained by observing their influence on the catalytic hydrolysis of a peptide substrate by the zinc enzyme carboxypeptidase A. The pH-dependence of Ki shows that binding is maximal between two pKa values: one is that of the phenol group of the inhibitor, and the other uniformly has a value of 6, the pKa of a Zn(2+)-bound water molecule on the enzyme in the absence of substrate or inhibitor. This is the dependence expected if phenolate binds to th

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30

Chapman, H. A., and O. L. Stone. "Characterization of a macrophage-derived plasminogen-activator inhibitor. Similarities with placental urokinase inhibitor." Biochemical Journal 230, no. 1 (August 15, 1985): 109–16. http://dx.doi.org/10.1042/bj2300109.

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Human and mouse macrophages release a fibrinolytic inhibitor after stimulation by endotoxin in vitro. The released mouse inhibitor was indistinguishable in size by molecular-sieve chromatography from an intracellular form (approx. 50 kDa), and both inhibitors blocked urokinase directly as judged by a 125I-plasminogen conversion assay. The intracellular inhibitor was found mostly to dissociate from 125I-urokinase during sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under reduced conditions, but a dodecyl sulphate-stable complex at 65-67 kDa was observed. Because of similarities in

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31

Liu, S. Q., E. Ries, and P. A. Knauf. "Effects of external pH on binding of external sulfate, 4.4-dinitro-stilbene-2,2'-disulfonate (DNDS), and chloride to the band 3 anion exchange protein." Journal of General Physiology 107, no. 2 (February 1, 1996): 293–306. http://dx.doi.org/10.1085/jgp.107.2.293.

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A model in which two positively-charged titratable sites enhance the affinity for anionic substrates can explain the increase in external iodide dissociation constant (K(O)(I)) with increasing pH(O) (Liu, S. J., F.-Y. Law, and P.A. Knauf. 1996.f Gen.Physiol. 107:271-291). If sulfate binds to the same external site as I-, this model predicts that the SO(4)= dissociation constant (K(O)(S)) should also increase. The data at pH 0 8.5 to 10 fit this prediction, and the pK for the titration is not significantly different from that (pKc) for the low-pK group that affects K(O)(1). The dissociation con

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32

Faller, B., S. Dirrig, M. Rabaud, and J. G. Bieth. "Kinetics of the inhibition of human pancreatic elastase by recombinant eglin c. Influence of elastin." Biochemical Journal 270, no. 3 (September 15, 1990): 639–44. http://dx.doi.org/10.1042/bj2700639.

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Recombinant eglin c is a potent reversible inhibitor of human pancreatic elastase. At pH 7.4 and 25 degrees C, kass. = 7.3 x 10(5) M-1.s-1, kdiss. = 2.7 x 10(-4) s-1 and Ki = 3.7 x 10(-10) M. Stopped-flow kinetic indicate that the formation of the stable enzyme-inhibitor complex is not preceded by a fast pre-equilibrium complex or that the latter has a dissociation constant greater than 0.3 microM. The elastase-eglin c complex is much less stable at pH 5.0 and 25 degrees C, where kdiss. = 1.1 x 10(-2) s-1 and Ki = 7.3 x 10(-8) M. At pH 7.4 the activation energy for kass. is 43.9 kJ.mol-1 (10.5

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33

Yoshino, M. "A graphical method for determining inhibition parameters for partial and complete inhibitors." Biochemical Journal 248, no. 3 (December 15, 1987): 815–20. http://dx.doi.org/10.1042/bj2480815.

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A new simple graphical method is described for the determination of inhibition type and kinetic parameters of an enzyme reaction without any replot. The method consists of plotting experimental data as v/(vo-v) versus the reciprocal of the inhibitor concentration at different substrate concentrations, where v and vo represent the velocity in the presence and in the absence of the inhibitor respectively with a given concentration of the substrate. Partial inhibition gives straight lines that converge on the abscissa at a point away from the origin, whereas complete inhibition gives lines that g

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34

Williams, H. R., T. Y. Lin, M. A. Navia, J. P. Springer, and K. Hoogsteen. "Pig pancreatic anhydro-elastase. Role of the serine-195 hydroxy group in the binding of inhibitors and substrate." Biochemical Journal 242, no. 1 (February 15, 1987): 267–73. http://dx.doi.org/10.1042/bj2420267.

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The binding constants of a number of ligands were measured for pancreatic elastase (PE) and anhydro-elastase (AE) in order to assess the contribution of Ser-195 to substrate and inhibitor binding by PE. AE was purified by affinity chromatography on a column containing immobilized turkey ovomucoid inhibitor. The AE had 0.1 +/- 0.1% of the activity of the native enzyme and contained 0.8 +/- 0.06 residue of dehydroalanine per molecule. A difference electron-density map, derived from an X-ray crystallographic analysis of AE, showed that the modified residue was Ser-195. The complexing of 3-carboxy

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35

Volpe, P., B. H. Alderson-Lang, and G. A. Nickols. "Regulation of inositol 1,4,5-trisphosphate-induced Ca2+ release. I. Effect of Mg2+." American Journal of Physiology-Cell Physiology 258, no. 6 (June 1, 1990): C1077—C1085. http://dx.doi.org/10.1152/ajpcell.1990.258.6.c1077.

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Canine cerebellar membranes were fractionated by differential centrifugation into a crude mitochondrial pellet (P2) and a crude microsomal pellet (P3). The effect of Mg2+ on inositol 1,4,5-trisphosphate (IP3)-induced Ca2+ release and [3H]IP3 binding was assessed. Mg2+ inhibited IP3-induced Ca2+ release in a concentration-dependent manner. Mg2+ influenced both the extent of IP3-induced Ca2+ release and the apparent affinity for IP3. A 10-fold change of free Mg2+ (from approximately 30 to approximately 300 microM) reduced the extent of Ca2+ release by two- to threefold and shifted the apparent M

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36

Nazir, Yasir, Hummera Rafique, Sadia Roshan, Shazia Shamas, Zaman Ashraf, Muhammad Rafiq, Tehreem Tahir, Zia-Ur-Rahman Qureshi, Alvina Aslam, and Muhammad Hassham Hassan Bin Asad. "Molecular Docking, Synthesis, and Tyrosinase Inhibition Activity of Acetophenone Amide: Potential Inhibitor of Melanogenesis." BioMed Research International 2022 (January 11, 2022): 1–10. http://dx.doi.org/10.1155/2022/1040693.

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Tyrosinase and its related proteins are responsible for pigmentation disorders, and inhibiting tyrosinase is an established strategy to treat hyperpigmentation. The carbonyl scaffolds can be effective inhibitors of tyrosinase activity, and the fact that both benzoic and cinnamic acids are safe natural substances with such a scaffolded structure, it was speculated that hydroxyl-substituted benzoic and cinnamic acid derivatives may exhibit potent tyrosinase inhibitory activity. These moieties were incorporated into new chemotypes that displayed in vitro inhibitory effect against mushroom tyrosin

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37

Crawford, Jeremie J., Joshua W. Hollett, and Douglas B. Craig. "Determination of the inhibitor dissociation constant of an individual unmodified enzyme molecule in free solution." ELECTROPHORESIS 37, no. 15-16 (June 29, 2016): 2217–25. http://dx.doi.org/10.1002/elps.201600201.

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38

Chen, C. K., T. J. McDonald, and E. E. Daniel. "Galanin receptor in plasma membrane of canine small intestinal circular muscle." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 1 (January 1, 1994): G113—G117. http://dx.doi.org/10.1152/ajpgi.1994.266.1.g113.

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High-affinity binding sites for galanin were identified and characterized in plasma membrane of circular muscle from canine small intestine using 125I-radioiodinated synthetic porcine galanin. Scatchard analysis indicated a high-affinity binding site on plasma membrane with a dissociation constant (Kd) of 0.58 nM and a binding capacity of 389 fmol/mg. Unlabeled galanin or NH2-terminal galanin fragments competitively inhibited the binding of 125I-galanin in a concentration-dependent manner, whereas the COOH-terminal fragment was inactive. Computer analysis of competitive binding data suggested

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39

Takai, A., Y. Ohno, T. Yasumoto, and G. Mieskes. "Estimation of the rate constants associated with the inhibitory effect of okadaic acid on type 2A protein phosphatase by time-course analysis." Biochemical Journal 287, no. 1 (October 1, 1992): 101–6. http://dx.doi.org/10.1042/bj2870101.

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As is often the case with tightly binding inhibitors, okadaic acid produces its inhibitory effect on type 2A protein phosphatase (PP2A) in a time-dependent manner. We measured the rate constants associated with the binding of okadaic acid to PP2A by analysing the time-course of the reduction of the p-nitrophenyl phosphate (pNPP) phosphatase activity of the enzyme after application of okadaic acid. The rate constants for dissociation of okadaic acid from PP2A were also estimated from the time-course of the recovery of the activity from inhibition by okadaic acid after addition of a mouse IgG1 m

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40

Wierzchowski, Jacek, Agnieszka Bzowska, Katarzyna Stępniak, and David Shugar. "Interactions of Calf Spleen Purine Nucleoside Phosphorylase with 8-Azaguanine, and a Bisubstrate Analogue Inhibitor: Implications for the Reaction Mechanism." Zeitschrift für Naturforschung C 59, no. 9-10 (October 1, 2004): 713–25. http://dx.doi.org/10.1515/znc-2004-9-1017.

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Abstract Interactions of calf spleen purine nucleoside phosphorylase (PNP) with a non-typical substrate, 8-azaguanine (8-azaG), and a bisubstrate analogue inhibitor, 9-(2-phosphonylmethoxyethyl)- 8-azaguanine (PME-azaG), were investigated by means of steady-state fluorescence spectroscopy. Both 8-azaG and PME-azaG form fluorescent complexes with the enzyme, and dissociation constants are comparable to the appropriate parameters (Km or Ki) obtained from kinetic measurements. PME-azaG inhibits both the phosphorolytic and synthetic pathway of the reaction in a competitive mode. The complex of 8-a

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41

Zaborska, W., M. Leszko, M. Kot, and A. Juszkiewicz. "The enthalpimetric determination of inhibition constants for the inhibition of urease by acetohydroxamic acid." Acta Biochimica Polonica 44, no. 1 (March 31, 1997): 89–98. http://dx.doi.org/10.18388/abp.1997_4444.

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The effect of concentration of acetohydroxamic acid (AHA) on inhibition of jack bean urease in phosphate buffer, pH 7.0, at 25 degrees C, was studied. The measurements were performed at urease concentration of 2.5 mg/100 cm3 for concentrations of urea and AHA ranging in the range of 2-50 mmol dm-3 and 0.25-10 mmol dm-3, respectively. The reactions were monitored by two techniques: analytical and enthalpimetric. For the analytical technique the growth of ammonia concentration in the course of the reaction was determined. From the recorded progress curves the following parameters were calculated

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42

ALDERTON, Wendy K., Angela BOYHAN, and Peter N. LOWE. "Nitroarginine and tetrahydrobiopterin binding to the haem domain of neuronal nitric oxide synthase using a scintillation proximity assay." Biochemical Journal 332, no. 1 (May 15, 1998): 195–201. http://dx.doi.org/10.1042/bj3320195.

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Nitric oxide synthases (NOS) have a bidomain structure comprised of an N-terminal oxygenase domain and a C-terminal reductase domain. The oxygenase domain binds haem, (6R)-5,6,7,8-tetrahydro-l-biopterin (tetrahydrobiopterin) and arginine, is the site where nitric oxide synthesis takes place and contains determinants for dimeric interactions. A novel scintillation proximity assay has been established for equilibrium and kinetic measurements of substrate, inhibitor and cofactor binding to a recombinant N-terminal haem-binding domain of rat neuronal NOS (nNOS). Apparent Kd values for nNOS haem-do

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43

Saboury, A. A., A. Divsalar, G. Ataie, M. Amanlou, A. A. Moosavi-Movahedi, and G. H. Hakimelahi. "Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry." Acta Biochimica Polonica 50, no. 3 (September 30, 2003): 849–55. http://dx.doi.org/10.18388/abp.2003_3676.

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Kinetic and thermodynamic studies were made on the effect of caffeine on the activity of adenosine deaminase in 50 mM sodium phosphate buffer, pH 7.5, using UV spectrophotometry and isothermal titration calorimetry (ITC). An uncompetitive inhibition was observed for caffeine. A graphical fitting method was used for determination of binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to 350 microM by the microcalorimetry method, which agrees well with the value of 342 microM for the inhibition constan

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44

Capitani, Guido, Darla L. McCarthy, Heinz Gut, Markus G. Grütter, and Jack F. Kirsch. "Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor l-Aminoethoxyvinylglycine." Journal of Biological Chemistry 277, no. 51 (September 11, 2002): 49735–42. http://dx.doi.org/10.1074/jbc.m208427200.

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The 1.6-Å crystal structure of the covalent ketimine complex of apple 1-aminocyclopropane-1-carboxylate (ACC) synthase with the potent inhibitorl-aminoethoxyvinylglycine (AVG) is described. ACC synthase catalyzes the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. AVG is widely used in plant physiology studies to inhibit the activity of ACC synthase. The structural assignment is supported by the fact that the complex absorbs maximally at 341 nm. These results are not

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45

Perilli, Mariagrazia, Alisia Mancini, Giuseppe Celenza, Carlo Bottoni, Pierangelo Bellio, Alessia Sabatini, Letizia Di Pietro, Fabrizia Brisdelli, Bernardetta Segatore та Gianfranco Amicosante. "Kinetic Study of the Effect of Histidines 240 and 164 on TEM-149 Enzyme Probed by β-Lactam Inhibitors". Antimicrobial Agents and Chemotherapy 58, № 10 (4 серпня 2014): 6294–96. http://dx.doi.org/10.1128/aac.02950-14.

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ABSTRACTIn the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149H240, and TEM-149H164-H240versus a large panel of inhibitors/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149H240, and TEM-149H164-H240β-lactamases, and theKi(inhibition constant),K(dissociation constant of the Henri-Michaelis complex),k+2andk+3(first-order acylation and deacylation constants, respectively), andk+2/Kvalues were calculated.

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46

Maqtari, Maher Ali, and A. B. Mohamed Saad. "Screening and Purification of a Chymotrypsin Inhibitor from Entrolobium Saman Seeds." Sultan Qaboos University Journal for Science [SQUJS] 15 (December 1, 2010): 19. http://dx.doi.org/10.24200/squjs.vol15iss0pp19-29.

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A chymotrypsin inhibitor was isolated and purified from the seeds of Enterolobium saman (Leguminaceae family) by extraction with 100 mM phosphate buffer, heat treatment, ammonium sulphate precipitation, ion-exchange chromatography on DEAEcellulose and filtration through Sephadex G-75. The final preparation appeared to be homogeneous by both chromatographic and electrophoretic analyses. ESCI had a molecular weight of about 17,890 and an isoelectric point of 5.8. ESCI inhibited bovine chymotrypsin at an inhibitor-enzyme molar ratio of 1:2. The inhibition mode of chymotrypsin inhibitor was compet

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47

Kanalas, J. J. "Characterization of plasminogen system on rat yolk sac carcinoma (L2) cells." American Journal of Physiology-Cell Physiology 268, no. 2 (February 1, 1995): C442—C448. http://dx.doi.org/10.1152/ajpcell.1995.268.2.c442.

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The plasminogen (Plg) system on rat yolk sac carcinoma (L2) cells was characterized by zymography, Western and immunoprecipitation analysis, reverse-transcriptase polymerase chain reaction, binding, and activity assays. The L2 cells produced tissue Plg activator but not urokinase Plg activator and contained RNA for Plg activator inhibitor 1, but Plg activator inhibitor 1 was not detectable by zymography or Western analysis and contained the receptor for urokinase Plg activator. Plg bound to the cells in a saturable manner when plasmin inhibitors were present with a dissociation constant of 1.3

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48

Nycander, M., and I. Björk. "Evidence by chemical modification that tryptophan-104 of the cysteine-proteinase inhibitor chicken cystatin is located in or near the proteinase-binding site." Biochemical Journal 271, no. 1 (October 1, 1990): 281–84. http://dx.doi.org/10.1042/bj2710281.

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The single tryptophan residue Trp-104 of chicken cystatin was modified with a 2-hydroxy-5-nitrobenzyl group. The change of the absorption spectrum of this group on binding of the modified cystatin to papain indicated a decreased environmental polarity of the probe. The modified inhibitor had about a 10(5)-fold lower affinity for papain than had intact cystatin, this being due to a higher dissociation rate constant. These results show that Trp-104 of cystatin is located in or near the proteinase-binding site of the inhibitor, in agreement with a model proposed from computer docking Experiments.

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49

Stratmann, Bernd, Martin Farr, and Harald Tschesche. "Characterization of C-Terminally Truncated Human Tissue Inhibitor of Metalloproteinases-4 Expressed in Pichia pastoris." Biological Chemistry 382, no. 6 (June 27, 2001): 987–91. http://dx.doi.org/10.1515/bc.2001.124.

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Abstract The tight regulation of extracellular matrix remodeling and degradation is of great importance in physiological processes like development and morphogenesis, as well as in pathological situations like tumor invasion and metastasis. Tissue inhibitors of metalloproteinases (TIMPs) are the naturally occuring inhibitors of matrix metalloproteinases, which are involved in matrix turnover. In this report we describe the cloning of human TIMP-4 from a human adenocarcinoma and an osteosarcoma cell line and the expression of the inhibitory domain in the methylotrophic yeast Pichia pastoris. Th

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50

Prystay, Linda, Mylene Gosselin, and Peter Banks. "Determination of Equilibrium Dissociation Constants in Fluorescence Polarization." Journal of Biomolecular Screening 6, no. 3 (June 2001): 141–50. http://dx.doi.org/10.1177/108705710100600304.

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A simple mathematical model (the FP Kd model) is used to generate the dissociation equilibrium constant (Kd) for G protein-coupled receptor-ligand binding measured using fluorescence polarization (FP) saturation curve analysis. The model generates data that may be analyzed by the method of Scatchard. The validity of the FP Kd model is proven in six model systems in which the modeled Kd values are within a factor of 5 of inhibitory equilibrium constant values obtained from radioligand competition assays.

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