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Journal articles on the topic 'Tryptophan residue'

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Published: 4 June 2021

Last updated: 3 February 2022

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1

Strøm, Morten B., Bengt Erik Haug, Øystein Rekdal, Merete L. Skar, Wenche Stensen, and John S. Svendsen. "Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity." Biochemistry and Cell Biology 80, no. 1 (2002): 65–74. http://dx.doi.org/10.1139/o01-236.

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This review focuses on important structural features affecting the antimicrobial activity of 15-residue derivatives of lactoferricins. Our investigations are based on an alanine-scan of a 15-residue bovine lactoferricin derivative that revealed the absolute necessity of two tryptophan residues for antimicrobial activity. This "tryptophan-effect" was further explored in homologous derivatives of human, caprine, and porcine lactoferricins by the incorporation of one additional tryptophan residue, and by increasing the content of tryptophan in the bovine derivative to five residues. Most of the r

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2

Bruch, Thomas vom, and Klaus-Heinrich Röhm. "Fluorescence Properties of Hog Kidney Aminoacylase I." Zeitschrift für Naturforschung C 43, no. 9-10 (1988): 671–78. http://dx.doi.org/10.1515/znc-1988-9-1008.

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Abstract The state of the tryptophan residues of porcine kidney aminoacylase I (EC 3.5.1.14) was investigated by fluorescence spectroscopy and chemical modification. The pH-dependence of the fluorescence emission spectrum of the enzyme indicates that its native conformation prevails between pH 6 and 9.5. Within this range, the ionization of a residue with an apparent pKa of 7.1 quenches the enzyme fluorescence by about 15%. A similar reduction of fluorescence intensity accompanies the inactivation of aminoacylase I by treatment with N-bromosuccinimide in low excess. This suggests that in both

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3

Okada, Masahiro, Tomotoshi Sugita, and Ikuro Abe. "Posttranslational isoprenylation of tryptophan in bacteria." Beilstein Journal of Organic Chemistry 13 (February 22, 2017): 338–46. http://dx.doi.org/10.3762/bjoc.13.37.

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Posttranslational isoprenylation is generally recognized as a universal modification of the cysteine residues in peptides and the thiol groups of proteins in eukaryotes. In contrast, the Bacillus quorum sensing peptide pheromone, the ComX pheromone, possesses a posttranslationally modified tryptophan residue, and the tryptophan residue is isoprenylated with either a geranyl or farnesyl group at the gamma position to form a tricyclic skeleton that bears a newly formed pyrrolidine, similar to proline. The post-translational dimethylallylation of two tryptophan residues of a cyclic peptide, kawag

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4

Kuo, Soong Yu, May Whei Lin, Shih Sheng Jiang, Shu Hsien Hung, Chi Meng Tzeng, and Rong Long Pan. "A tryptophan residue involved in the inhibition of plant vacuolar H+-ATPase by 2-hydroxy-5-nitrobenzyl bromide." Functional Plant Biology 25, no. 6 (1998): 679. http://dx.doi.org/10.1071/pp98008.

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Treatment of the vacuolar H+ -ATPase from mung bean seedlings (Vigna radiata L.) with the tryptophan modifying agent 2-hydroxyl-5-nitrobenzyl bromide (HNBB), caused a progressive decline of the ATP hydrolysis activity and proton translocation in a time- and concentration-dependent manner. Dithiothreitol could not restore the inhibition of H+ -ATPase by HNBB, indicating possible involvement tryptophan, and not cysteine residues. Protection studies suggested that modified sites might not locate in the active domain. Kinetic analysis shows that Vmax but not Km of H+ -ATPase was changed by HNBB. T

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5

Sarkar, Sayani, Adaitya Prasad Behera, Prateeka Borar, Prerana Agarwal Banka, and Ajit B. Datta. "Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases." Biochemical Journal 476, no. 10 (2019): 1465–82. http://dx.doi.org/10.1042/bcj20180883.

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Abstract Ubiquitin RING E3 ligases (E3s) catalyze ubiquitin (Ub) transfer to their substrates by engaging E2∼Ub intermediates with the help of their RING domains. Different E3s have been found to contain a conserved tryptophan residue in their RING that plays an essential role in E2 binding and, hence, enzymatic activity. Many active E3s, however, lack this specific residue. We mined through the existing data to observe that the conservation of the tryptophan and quaternary organization of the RING domains are remarkably correlated. Monomeric RINGs possess the tryptophan while all well-charact

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6

Dementieva, Ekaterina I., Elena A. Fedorchuk, Lubov Yu Brovko, Alexander P. Savitskii, and Natalya N. Ugarova. "Fluorescent Properties of Firefly Luciferases and Their Complexes with Luciferin." Bioscience Reports 20, no. 1 (2000): 21–30. http://dx.doi.org/10.1023/a:1005579016387.

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Fluorescence of luciferases from Luciola mingrelica (single tryptophanresidue, Trp-419) and Photinus pyralis (two tryptophan residues, Trp-417,Trp-426) was studied. Analysis of quenching of tryptophan fluorescenceshowed that the tryptophan residue conserved in all luciferases is notaccessible for charged quenchers, which is explained by the presence ofpositively and negatively charged amino acid residues in the close vicinityto it. An effective energy transfer from tryptophan to luciferin wasobserved during quenching of tryptophan fluorescence of both luciferaseswith luciferin. From the data o

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7

MALOVRH, Petra, Ariana BARLIĆ, Zdravko PODLESEK, Peter MAĆEK, Gianfranco MENESTRINA, and Gregor ANDERLUH. "Structure–function studies of tryptophan mutants of equinatoxin II, a sea anemone pore-forming protein." Biochemical Journal 346, no. 1 (2000): 223–32. http://dx.doi.org/10.1042/bj3460223.

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Equinatoxin II (EqtII) is a eukaryotic cytolytic toxin that avidly creates pores in natural and model lipid membranes. It contains five tryptophan residues in three different regions of the molecule. In order to study its interaction with the lipid membranes, three tryptophan mutants, EqtII Trp45, EqtII Trp116/117 and EqtII Trp149, were prepared in an Escherichia coli expression system [here, the tryptophan mutants are classified according to the position of the remaining tryptophan residue(s) in each mutated protein]. They all possess a single intrinsic fluorescent centre. All mutants were le

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8

Friedman, M. L., K. T. Schlueter, T. L. Kirley, and H. B. Halsall. "Fluorescence quenching of human orosomucoid. Accessibility to drugs and small quenching agents." Biochemical Journal 232, no. 3 (1985): 863–67. http://dx.doi.org/10.1042/bj2320863.

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The fluorescence behaviour of human orosomucoid was investigated. The intrinsic fluorescence was more accessible to acrylamide than to the slightly larger succinimide, indicating limited accessibility to part of the tryptophan population. Although I- showed almost no quenching, that of Cs+ was enhanced, and suggested a region of negative charge proximal to an emitting tryptophan residue. Removal of more than 90% of sialic acid from the glycan chains led to no change in the Cs+, I-, succinimide or acrylamide quenching, indicating that the negatively charged region originates with the protein co

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9

Swamy, Musti Joginadha, and Avadhesha Surolia. "Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding." Bioscience Reports 9, no. 2 (1989): 189–98. http://dx.doi.org/10.1007/bf01115995.

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Modification of tryptophan side chains of soybean agglutinin (SBA) with N-bromosuccinimide results in a loss of the hemagglutinating and carbohydrate binding activities of the protein. One residue/subunit is probably essential for the binding activity. Modification leads to a large decrease in the fluorescene of the protein accompained by a blue shift. Iodide ion quenching of the protein fluorescence shows that saccharide binding results in a decreased accessibility of some of the tryptophan side chains. These results strongly point towards the involvement of tryptophan residues in the active

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10

Zhang, Z., K. Ostanin, and R. L. Van Etten. "Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase." Acta Biochimica Polonica 44, no. 4 (1997): 659–72. http://dx.doi.org/10.18388/abp.1997_4368.

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Because tryptophans are found as part of the phosphate binding sites in a number of proteins, human prostatic acid phosphatase (hPAP) was examined for the presence and the role of essential tryptophan residues. The pH dependence of the intrinsic fluorescence of hPAP resembled the kinetic pH dependence. Chemical modification by N-bromosuccinimide (NBS) resulted in an inactivation of the enzyme and produced a characteristic reduction of the protein absorbance at 280 nm. Two tryptophans per subunit were modified, and this was accompanied by an apparently complete loss of enzymatic activity. In th

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11

Gitlin, G., E. A. Bayer, and M. Wilchek. "Studies on the biotin-binding site of avidin. Tryptophan residues involved in the active site." Biochemical Journal 250, no. 1 (1988): 291–94. http://dx.doi.org/10.1042/bj2500291.

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Egg-white avidin was modified with the tryptophan-specific reagent 2-hydroxy-5-nitrobenzyl bromide. The complete loss of biotin-binding activity was achieved upon modification of an average of one tryptophan residue per avidin subunit. The identity of the modified residues was determined by isolating the relevant tryptic and chymotryptic peptides from CNBr-cleaved avidin fragments. The results demonstrate that Trp-70 and Trp-110 are modified in approximately equivalent proportions. It is believed that these residues are located in the active site of avidin and take part in the binding of bioti

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12

Salzwedel, Karl, John T. West, and Eric Hunter. "A Conserved Tryptophan-Rich Motif in the Membrane-Proximal Region of the Human Immunodeficiency Virus Type 1 gp41 Ectodomain Is Important for Env-Mediated Fusion and Virus Infectivity." Journal of Virology 73, no. 3 (1999): 2469–80. http://dx.doi.org/10.1128/jvi.73.3.2469-2480.1999.

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ABSTRACT Mutations were introduced into the ectodomain of the human immunodeficiency virus type 1 (HIV-1) transmembrane envelope glycoprotein, gp41, within a region immediately adjacent to the membrane-spanning domain. This region, which is predicted to form an α-helix, contains highly conserved hydrophobic residues and is unusually rich in tryptophan residues. In addition, this domain overlaps the epitope of a neutralizing monoclonal antibody, 2F5, as well as the sequence corresponding to a peptide, DP-178, shown to potently neutralize virus. Site-directed mutagenesis was used to create delet

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13

Laco, Gary S., and Yves Pommier. "Role of a tryptophan anchor in human topoisomerase I structure, function and inhibition." Biochemical Journal 411, no. 3 (2008): 523–30. http://dx.doi.org/10.1042/bj20071436.

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Human Top1 (topoisomerase I) relaxes supercoiled DNA during cell division and transcription. Top1 is composed of 765 amino acids and contains an unstructured N-terminal domain of 200 amino acids, and a structured functional domain of 565 amino acids that binds and relaxes supercoiled DNA. In the present study we examined the region spanning the junction of the N-terminal domain and functional domain (junction region). Analysis of several published Top1 structures revealed that three tryptophan residues formed a network of aromatic stacking interactions and electrostatic interactions that ancho

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14

HE, Qing-Yu, Anne B. MASON, Barbara A. LYONS, et al. "Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe." Biochemical Journal 354, no. 2 (2001): 423–29. http://dx.doi.org/10.1042/bj3540423.

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Human serum transferrin N-lobe (hTF/2N) contains three conserved tryptophan residues, Trp8, Trp128 and Trp264, located in three different environments. The present report addresses the different contributions of the three tryptophan residues to the UV–visible, fluorescence and NMR spectra of hTF/2N and the effect of the mutations at each tryptophan residue on the iron-binding properties of the protein. Trp8 resides in a hydrophobic box containing a cluster of three phenylalanine side chains and is H bonded through the indole N to an adjacent water cluster lying between two β-sheets containing

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15

Baik, Lisa S., David D. Au, Ceazar Nave, Alexander J. Foden, Wendy K. Enrriquez-Villalva, and Todd C. Holmes. "Distinct mechanisms of Drosophila CRYPTOCHROME-mediated light-evoked membrane depolarization and in vivo clock resetting." Proceedings of the National Academy of Sciences 116, no. 46 (2019): 23339–44. http://dx.doi.org/10.1073/pnas.1905023116.

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Drosophila CRYPTOCHROME (dCRY) mediates electrophysiological depolarization and circadian clock resetting in response to blue or ultraviolet (UV) light. These light-evoked biological responses operate at different timescales and possibly through different mechanisms. Whether electron transfer down a conserved chain of tryptophan residues underlies biological responses following dCRY light activation has been controversial. To examine these issues in in vivo and in ex vivo whole-brain preparations, we generated transgenic flies expressing tryptophan mutant dCRYs in the conserved electron transf

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16

RUDDOCK, Lloyd W., Timothy R. HIRST, and Robert B. FREEDMAN. "pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate." Biochemical Journal 315, no. 3 (1996): 1001–5. http://dx.doi.org/10.1042/bj3151001.

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A decapeptide containing two cysteine residues at positions 3 and 8 has been designed for use in monitoring the disulphide bond-forming activity of thiol:disulphide oxidoreductases. The peptide contains a tryptophan residue adjacent to one of the cysteine residues and an arginine residue adjacent to the other. Oxidation of this dithiol peptide to the disulphide state is accompanied by a significant change in tryptophan fluorescence emission intensity. This fluorescence quenching was used as the basis for monitoring the disulphide bond-forming activity of the enzymes protein disulphide-isomeras

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Zavorotinskaya, Tatiana, and Lorraine M. Albritton. "A Hydrophobic Patch in Ecotropic Murine Leukemia Virus Envelope Protein Is the Putative Binding Site for a Critical Tyrosine Residue on the Cellular Receptor." Journal of Virology 73, no. 12 (1999): 10164–72. http://dx.doi.org/10.1128/jvi.73.12.10164-10172.1999.

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ABSTRACT In the receptor for ecotropic murine leukemia viruses, tyrosine 235 contributes a critical hydrophobic side chain to the virus-receptor interaction (14). Here we report that tryptophan 142 in ecotropic Moloney murine leukemia virus envelope protein is essential to virus binding and infection. Replacement of tryptophan 142 by alanine or serine resulted in misfolding. However, replacement by methionine (W142M) allowed correct folding of the majority of glycoprotein molecules. W142M virus showed a marked reduction in virus binding and was almost noninfectious, suggesting that tryptophan

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18

Zhou, Huaijin, and Joe Lutkenhaus. "Membrane Binding by MinD Involves Insertion of Hydrophobic Residues within the C-Terminal Amphipathic Helix into the Bilayer." Journal of Bacteriology 185, no. 15 (2003): 4326–35. http://dx.doi.org/10.1128/jb.185.15.4326-4335.2003.

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ABSTRACT MinD binds to phospholipid vesicles in the presence of ATP and is released by MinE, which stimulates the MinD ATPase. Membrane binding requires a short conserved C-terminal region, which has the potential to form an amphipathic helix. This finding has led to a model in which the binding of ATP regulates the formation or accessibility of this helix, which then embeds in the membrane bilayer. To test this model, we replaced each of the four hydrophobic residues within this potential helix with tryptophan or a charged residue. Introduction of a negatively charged amino acid decreased mem

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Gitlin, G., E. A. Bayer, and M. Wilchek. "Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site." Biochemical Journal 256, no. 1 (1988): 279–82. http://dx.doi.org/10.1042/bj2560279.

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Streptavidin, the non-glycosylated bacterial analogue of the egg-white glycoprotein avidin, was modified with the tryptophan-specific reagent 2-hydroxy-5-nitrobenzyl (Hnb) bromide. As with avidin, complete loss of biotin-binding activity was achieved upon modification of an average of one tryptophan residue per streptavidin subunit. Tryptic peptides obtained from an Hnb-modified streptavidin preparation were fractionated by reversed-phase h.p.l.c., and three major Hnb-containing peptide fractions were isolated. Amino acid and N-terminal sequence analysis revealed that tryptophan residues 92, 1

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20

Kovář, Jan, and Ivana Matysková. "Effect of modification of certain amino acid residues on enzyme activity of D-3-hydroxybutyrate dehydrogenase from bacterium Paracoccus denitrificans." Collection of Czechoslovak Chemical Communications 52, no. 7 (1987): 1872–77. http://dx.doi.org/10.1135/cccc19871872.

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We examined the effect of several modifying reagents on the activity of the title enzyme. The results show that one histidine residue participates in the interaction of the enzyme with the substrate; one cysteine residue binds near to the nicotine amide moiety of the coenzyme molecule and its role is to induce conformational changes leading to the formation of enzyme aggregates with an increased catalytic power. The enzyme does not contain essential tyrosine and tryptophan residues. The results of the experiments with the modification of additional amino acid residues permit us to make prelimi

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Cruz-Vera, Luis R., Rui Yang, and Charles Yanofsky. "Tryptophan Inhibits Proteus vulgaris TnaC Leader Peptide Elongation, Activating tna Operon Expression." Journal of Bacteriology 191, no. 22 (2009): 7001–6. http://dx.doi.org/10.1128/jb.01002-09.

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ABSTRACT Expression of the tna operon of Escherichia coli and of Proteus vulgaris is induced by l-tryptophan. In E. coli, tryptophan action is dependent on the presence of several critical residues (underlined) in the newly synthesized TnaC leader peptide, WFNIDXXL/IXXXXP. These residues are conserved in TnaC of P. vulgaris and of other bacterial species. TnaC of P. vulgaris has one additional feature, distinguishing it from TnaC of E. coli; it contains two C-terminal lysine residues following the conserved proline residue. In the present study, we investigated l-tryptophan induction of the P.

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CEZARI, Maria Helena S., Luciano PUZER, Maria Aparecida JULIANO, Adriana K. CARMONA, and Luiz JULIANO. "Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides." Biochemical Journal 368, no. 1 (2002): 365–69. http://dx.doi.org/10.1042/bj20020840.

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We have examined in detail the specificity of the subsites S1, S2, S1′ and S2′ for the carboxydipeptidase activity of cathepsin B by synthesizing and assaying four series of internally quenched fluorescent peptides based on the sequence Dnp-GFRFW-OH, where Dnp (2,4-dinitrophenyl) is the quenching group of the fluorescence of the tryptophan residue. Each position, except the glycine, was substituted with 15 different naturally occurring amino acids. Based on the results we obtained, we also synthesized efficient and sensitive substrates that contained o-aminobenzoic acid and 3-Dnp-(2,3-diaminop

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Cruz-Vera, Luis R., and Charles Yanofsky. "Conserved Residues Asp16 and Pro24 of TnaC-tRNAPro Participate in Tryptophan Induction of tna Operon Expression." Journal of Bacteriology 190, no. 14 (2008): 4791–97. http://dx.doi.org/10.1128/jb.00290-08.

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ABSTRACT In Escherichia coli, interactions between the nascent TnaC-tRNAPro peptidyl-tRNA and the translating ribosome create a tryptophan binding site in the ribosome where bound tryptophan inhibits TnaC-tRNAPro cleavage. This inhibition delays ribosome release, thereby inhibiting Rho factor binding and action, resulting in increased tna operon transcription. Replacing Trp12 of TnaC with any other amino acid residue was previously shown to prevent tryptophan binding and induction of tna operon expression. Genome-wide comparisons of TnaC amino acid sequences identify Asp16 and Pro24, as well a

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Garnir, Kevin, Sandra Estalayo-Adrián, Rémy Lartia, et al. "Parameters influencing the photo-induced electron transfer from tryptophan-containing peptides to a RuII complex: a systematic study." Faraday Discussions 185 (2015): 267–84. http://dx.doi.org/10.1039/c5fd00059a.

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Ruthenium(ii) polyazaaromatic complexes have gained interest in recent decades as biomolecular tools, especially in the development of new phototherapeutic agents. These light emissive Ru complexes based on π-deficient ligands were first designed to allow a photo-induced electron transfer (PET) with the guanine base in DNA since their <sup>3</sup>MLCT state is highly photo-oxidizing. Later the field of research was extended to proteins with the highlighting of a PET process with the tryptophan residue. This paper reports the kinetics of the luminescence quenching of [Ru(TAP)<sub>2</sub>phen]<s

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Hervé, F., M. T. Martin, K. Rajkowski, P. Dessen та N. Cittanova. "Participation of the lone tryptophan residue of rat α-foetoprotein in its drug-binding sites. Comparison with rat serum albumin". Biochemical Journal 244, № 1 (1987): 81–85. http://dx.doi.org/10.1042/bj2440081.

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The participation in drug binding of the lone tryptophan residue of rat alpha-foetoprotein (alpha-FP) and serum albumin, the two main transport proteins of foetal serum, has been studied by two different techniques. Firstly, the effect on phenylbutazone and warfarin binding of the chemical derivatization of the lone tryptophan residue of both proteins by 2-nitrophenylsulphonyl chloride (NPS) was studied. Secondly, the effect of phenylbutazone binding on the intrinsic fluorescence of the tryptophan residue of rat alpha-FP and albumin was investigated. The specific modification of the proteins b

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LECONA, Emilio, Javier TURNAY, Nieves OLMO, et al. "Structural and functional characterization of recombinant mouse annexin A11: influence of calcium binding." Biochemical Journal 373, no. 2 (2003): 437–49. http://dx.doi.org/10.1042/bj20021721.

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Annexin A11 is one of the 12 vertebrate subfamilies in the annexin superfamily of calcium/phospholipid-binding proteins, distinguishable by long, non-homologous N-termini rich in proline, glycine and tyrosine residues. As there is negligible structural information concerning this annexin subfamily apart from primary sequence data, we have cloned, expressed and purified recombinant mouse annexin A11 to investigate its structural and functional properties. CD spectroscopy reveals two main secondary-structure contributions, α-helix and random coil (approx. 30% each), corresponding mainly to the a

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Cosgriff, Angela J., Geoff Brasier, Jing Pi, Con Dogovski, Joseph P. Sarsero, and A. J. Pittard. "A Study of AroP-PheP Chimeric Proteins and Identification of a Residue Involved in Tryptophan Transport." Journal of Bacteriology 182, no. 8 (2000): 2207–17. http://dx.doi.org/10.1128/jb.182.8.2207-2217.2000.

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ABSTRACT In vivo recombination has been used to make a series of AroP-PheP chimeric proteins. Analysis of their respective substrate profiles and activities has identified a small region within span III of AroP which can confer on a predominantly PheP protein the ability to transport tryptophan. Site-directed mutagenesis of the AroP-PheP chimera, PheP, and AroP has established that a key residue involved in tryptophan transport is tyrosine at position 103 in AroP. Phenylalanine is the residue at the corresponding position in PheP. The use of PheP-specific antisera has shown that the inability

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Peyser, Y. Michael, Andras Muhlrad, and Moshe M. Werber. "Tryptophan-130 is the most reactive tryptophan residue in rabbit skeletal myosin subfragment-1." FEBS Letters 259, no. 2 (1990): 346–48. http://dx.doi.org/10.1016/0014-5793(90)80044-j.

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Xu, Lisheng, Fangkai Han, Zeng Dong, and Zhaojun Wei. "Engineering Improves Enzymatic Synthesis of L-Tryptophan by Tryptophan Synthase from Escherichia coli." Microorganisms 8, no. 4 (2020): 519. http://dx.doi.org/10.3390/microorganisms8040519.

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To improve the thermostability of tryptophan synthase, the molecular modification of tryptophan synthase was carried out by rational molecular engineering. First, B-FITTER software was used to analyze the temperature factor (B-factor) of each amino acid residue in the crystal structure of tryptophan synthase. A key amino acid residue, G395, which adversely affected the thermal stability of the enzyme, was identified, and then, a mutant library was constructed by site-specific saturation mutation. A mutant (G395S) enzyme with significantly improved thermal stability was screened from the satura

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Mukherjee, Manini, Ranendu Ghosh, Krishnananda Chattopadhyay, and Sanjib Ghosh. "pH-induced structural change of a multi-tryptophan protein MPT63 with immunoglobulin-like fold: identification of perturbed tryptophan residue/residues." Journal of Biomolecular Structure and Dynamics 33, no. 10 (2015): 2145–60. http://dx.doi.org/10.1080/07391102.2014.992043.

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Hassan, Karl A., Talal Souhani, Ronald A. Skurray, and Melissa H. Brown. "Analysis of Tryptophan Residues in the Staphylococcal Multidrug Transporter QacA Reveals Long-Distance Functional Associations of Residues on Opposite Sides of the Membrane." Journal of Bacteriology 190, no. 7 (2008): 2441–49. http://dx.doi.org/10.1128/jb.01864-07.

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ABSTRACT Tryptophan residues can possess a multitude of functions within a multidrug transport protein, e.g., mediating interactions with substrates or distal parts of the protein, or fulfilling a structural requirement, such as guiding the depth of membrane insertion. In this study, the nine tryptophan residues of the staphylococcal QacA multidrug efflux protein were individually mutated to alanine and phenylalanine, and the functional consequences of these changes were determined. Phenylalanine substitutions for each tryptophan residue were functionally tolerated. However, alanine modificati

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el Kebbaj, M. S., N. Latruffe, M. Monsigny та A. Obrenovitch. "Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence". Biochemical Journal 237, № 2 (1986): 359–64. http://dx.doi.org/10.1042/bj2370359.

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Interactions of D-beta-hydroxybutyrate dehydrogenase with phospholipids were investigated by both intrinsic- and extrinsic-fluorescence approaches. The intrinsic fluorescence, mainly caused by tryptophan residues, increased upon re-activation in the presence of phospholipids bearing a positive charge, i.e. phosphatidylcholine, but decreased in the presence of non-re-activating phospholipids with a negative charge. This indicates either that the environment of tryptophan residues is affected by charges rather than by hydrophobic chains of phospholipids, or that the enzyme undergoes different co

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Zhou, Hai-Meng, and Chen-Lu Tsou. "An essential tryptophan residue for rabbit muscle creatine kinase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 830, no. 1 (1985): 59–63. http://dx.doi.org/10.1016/0167-4838(85)90131-1.

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Sprenger, Janina, Catherine L. Lawson, Claes von Wachenfeldt, Leila Lo Leggio, and Jannette Carey. "Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan." Acta Crystallographica Section F Structural Biology Communications 77, no. 7 (2021): 215–25. http://dx.doi.org/10.1107/s2053230x21006142.

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The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand L-tryptophan (L-Trp) indicate that L-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts. This result is unexpected because the ligand binding-site residues arise from three separate polypeptide chains in the domain-swapped form. This work represents the first published structure of a domain-swapped form of TrpR with L-Trp bound. The presented structures also show that the protein amino

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Sheth, Sujitraj, Aurélie Baron, Christian Herrero, Boris Vauzeilles, Ally Aukauloo, and Winfried Leibl. "Light-induced tryptophan radical generation in a click modular assembly of a sensitiser-tryptophan residue." Photochemical & Photobiological Sciences 12, no. 6 (2013): 1074. http://dx.doi.org/10.1039/c3pp50021g.

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Batra, R., and D. J. Manstein. "Functional Characterisation of Dictyostelium Myosin II with Conserved Tryptophanyl Residue 501 Mutated to Tyrosine." Biological Chemistry 380, no. 7-8 (1999): 1017–23. http://dx.doi.org/10.1515/bc.1999.126.

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AbstractWe created aDictyostelium discoideummyosin II mutant in which the highly conserved residue Trp-501 was replaced by a tyrosine residue. The mutant myosin alone, when expressed in aDictyosteliumstrain lacking the functional myosin II heavy chain gene, supported cytokinesis and multicellular development, processes which require a functional myosin inDictyostelium. Additionally, we expressed the W501Y mutant in the soluble myosin head fragment M761-2R (W501Y-2R) to characterise the kinetic properties of the mutant myosin motor domain. The affinity of the mutant myosin for actin was approxi

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Meyer, J., J. Gagnon, L. C. Sieker, A. Van Dorsselaer, and J. M. Moulis. "Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data." Biochemical Journal 271, no. 3 (1990): 839–41. http://dx.doi.org/10.1042/bj2710839.

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Rubredoxin isolated from the thermophilic bacterium Clostridium thermosaccharolyticum has been sequenced and crystallized. The 52-residue sequence is similar to those of rubredoxins occurring in other anaerobic bacteria, but displays some unique features, including a tryptophan residue in position 4, two consecutive proline residues in positions 25 and 26, and an aspartic acid residue in position 41. The molecular mass (5988 Da) of the native rubredoxin has been measured by electrospray-ionization m.s., thus establishing the applicability of the technique to this type of iron-sulphur protein.

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Cruz-Vera, Luis R., Aaron New, Catherine Squires, and Charles Yanofsky. "Ribosomal Features Essential for tna Operon Induction: Tryptophan Binding at the Peptidyl Transferase Center." Journal of Bacteriology 189, no. 8 (2007): 3140–46. http://dx.doi.org/10.1128/jb.01869-06.

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ABSTRACT Features of the amino acid sequence of the TnaC nascent peptide are recognized by the translating ribosome. Recognition leads to tryptophan binding within the translating ribosome, inhibiting the termination of tnaC translation and preventing Rho-dependent transcription termination in the tna operon leader region. It was previously shown that inserting an adenine residue at position 751 or introducing the U2609C change in 23S rRNA or introducing the K90W replacement in ribosomal protein L22 prevented tryptophan induction of tna operon expression. It was also observed that an adenine a

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Gitlin, G., I. Khait, E. A. Bayer, M. Wilchek, and K. A. Muszkat. "Studies on the biotin-binding sites of avidin and streptavidin. A chemically induced dynamic nuclear polarization investigation of the status of tyrosine residues." Biochemical Journal 259, no. 2 (1989): 493–98. http://dx.doi.org/10.1042/bj2590493.

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We applied the protein photochemically induced dynamic nuclear polarization (photo-c.i.d.n.p.) method to explore the conformation of the side chains of tyrosine, tryptophan and histidine residues in three biotin-binding proteins. The c.i.d.n.p. spectra of avidin, streptavidin and ‘core’ streptavidin were compared with those of their complexes with biotin and its derivatives. The data indicate that the single tyrosine residue (Tyr-33) of avidin is clearly inaccessible to the triplet flavin photo-c.i.d.n.p. probe. The same holds for all tryptophan and histidine side chains. Although the analogou

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GUTSCHE, Birgit, Christoph GRUN, Dieter SCHEUTZOW, and Markus HERDERICH. "Tryptophan glycoconjugates in food and human urine*." Biochemical Journal 343, no. 1 (1999): 11–19. http://dx.doi.org/10.1042/bj3430011.

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Evaluating the formation of tryptophan glycoconjugates other than well-established Amadori rearrangement products, HPLC-tandem MS (MS/MS) analysis of human urine collected from several healthy individuals proved the presence of one distinct tryptophan C-glycosyl compound [Horiuchi, Yonekawa, Iwahara, Kanno, Kurihara and Fujise (1994) J. Biochem. (Tokyo) 115, 362-366]. After isolation, unambiguous identification of this novel tryptophan metabolite as 2-(α-mannopyranosyl)-L-tryptophan was achieved by tandem MS combined with NMR spectroscopy including homonuclear COSY, heteronuclear multiple-bond

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Najmi, Mitra, Rongbao Zhao, Andras Fiser, and I. David Goldman. "Role of the tryptophan residues in proton-coupled folate transporter (PCFT-SLC46A1) function." American Journal of Physiology-Cell Physiology 311, no. 1 (2016): C150—C157. http://dx.doi.org/10.1152/ajpcell.00084.2016.

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The proton-coupled folate transporter (PCFT) mediates folate absorption across the brush-border membrane of the proximal small intestine and is required for folate transport across the choroid plexus into the cerebrospinal fluid. In this study, the functional role and accessibility of the seven PCFT Trp residues were assessed by the substituted-cysteine accessibility method. Six Trp residues at a lipid-aqueous interface tolerated Cys substitution in terms of protein stability and function. W85C, W202C, and W213C were accessible to N-biotinyl aminoethylmethanethiosulfonate; W48C and W299C were

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Kiziak, Christoph, and Andreas Stolz. "Identification of Amino Acid Residues Responsible for the Enantioselectivity and Amide Formation Capacity of the Arylacetonitrilase from Pseudomonas fluorescens EBC191." Applied and Environmental Microbiology 75, no. 17 (2009): 5592–99. http://dx.doi.org/10.1128/aem.00301-09.

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ABSTRACT The nitrilase from Pseudomonas fluorescens EBC191 converted (R,S)-mandelonitrile with a low enantioselectivity to (R)-mandelic acid and (S)-mandeloamide in a ratio of about 4:1. In contrast, the same substrate was hydrolyzed by the homologous nitrilase from Alcaligenes faecalis ATCC 8750 almost exclusively to (R)-mandelic acid. A chimeric enzyme between both nitrilases was constructed, which represented in total 16 amino acid exchanges in the central part of the nitrilase from P. fluorescens EBC191. The chimeric enzyme clearly resembled the nitrilase from A. faecalis ATCC 8750 in its

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Chen, Kuan-Chung, та Calvin Yu-Chian Chen. "In SilicoIdentification of Potent PPAR-γAgonists from Traditional Chinese Medicine: A Bioactivity Prediction, Virtual Screening, and Molecular Dynamics Study". Evidence-Based Complementary and Alternative Medicine 2014 (2014): 1–19. http://dx.doi.org/10.1155/2014/192452.

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The peroxisome proliferator-activated receptors (PPARs) related to regulation of lipid metabolism, inflammation, cell proliferation, differentiation, and glucose homeostasis by controlling the related ligand-dependent transcription of networks of genes. They are used to be served as therapeutic targets against metabolic disorder, such as obesity, dyslipidemia, and diabetes; especially, PPAR-γis the most extensively investigated isoform for the treatment of dyslipidemic type 2 diabetes. In this study, we filter compounds of traditional Chinese medicine (TCM) using bioactivities predicted by thr

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Arvidson, D. N., M. Shapiro, and P. Youderian. "Mutant tryptophan aporepressors with altered specificities of corepressor recognition." Genetics 128, no. 1 (1991): 29–35. http://dx.doi.org/10.1093/genetics/128.1.29.

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Abstract The Escherichia coli trpR gene encodes tryptophan aporepressor, which binds the corepressor ligand, L-tryptophan, to form an active repressor complex. The side chain of residue valine 58 of Trp aporepressor sits at the bottom of the corepressor (L-tryptophan) binding pocket. Mutant trpR genes encoding changes of Val58 to the other 19 naturally occurring amino acids were made. Each of the mutant proteins requires a higher intracellular concentration of tryptophan for activation of DNA binding than wild-type aporepressor. Whereas wild-type aporepressor is activated better by 5-methyltry

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Michaux, Julien, Jean-Marc Campagne, and Pascal Retailleau. "Synthesis of the Central Tryptophan-Leucine Residue of Celogentin C." Synlett 2008, no. 10 (2008): 1532–36. http://dx.doi.org/10.1055/s-2008-1078411.

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Bentley, David J., and Christopher J. Moody. "Asymmetric synthesis of the central tryptophan residue of stephanotic acid." Organic & Biomolecular Chemistry 2, no. 24 (2004): 3545. http://dx.doi.org/10.1039/b414996c.

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Pigault, Claire, and Dominique Gerard. "PHOTOLYSIS OF THE SINGLE TRYPTOPHAN RESIDUE OF EEL TROPONIN C." Photochemistry and Photobiology 48, no. 3 (1988): 349–51. http://dx.doi.org/10.1111/j.1751-1097.1988.tb02832.x.

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Thumser, A. E., and D. C. Wilton. "Characterization of binding and structural properties of rat liver fatty-acid-binding protein using tryptophan mutants." Biochemical Journal 300, no. 3 (1994): 827–33. http://dx.doi.org/10.1042/bj3000827.

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Rat liver fatty-acid-binding protein (FABP) does not contain tryptophan. Three mutant proteins have been produced in which a single tryptophan residue has been inserted by site-directed mutagenesis at positions 3 (F3W), 18 (F18W) and 69 (C69W). These tryptophans have been strategically located in order to provide fluorescent reporter groups to study the binding and structural characteristics of rat liver FABP. Two fluorescent fatty acid analogues, DAUDA (11-[(5-dimethylaminonaphthalene-1- sulphonyl)amino]undecanoic acid) and 3-[p-(6-phenyl)-hexa-1,3,5-trienyl]phenylpropionic acid, showed no si

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Monni, Roberto, André Al Haddad, Frank van Mourik, Gerald Auböck, and Majed Chergui. "Tryptophan-to-heme electron transfer in ferrous myoglobins." Proceedings of the National Academy of Sciences 112, no. 18 (2015): 5602–6. http://dx.doi.org/10.1073/pnas.1423186112.

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It was recently demonstrated that in ferric myoglobins (Mb) the fluorescence quenching of the photoexcited tryptophan 14 (*Trp14) residue is in part due to an electron transfer to the heme porphyrin (porph), turning it to the ferrous state. However, the invariance of *Trp decay times in ferric and ferrous Mbs raises the question as to whether electron transfer may also be operative in the latter. Using UV pump/visible probe transient absorption, we show that this is indeed the case for deoxy-Mb. We observe that the reduction generates (with a yield of about 30%) a low-valence Fe–porphyrin π [F

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Cowton, Vanessa M., Allan G. N. Angus, Sarah J. Cole, et al. "Role of Conserved E2 Residue W420 in Receptor Binding and Hepatitis C Virus Infection." Journal of Virology 90, no. 16 (2016): 7456–68. http://dx.doi.org/10.1128/jvi.00685-16.

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ABSTRACTHepatitis C virus (HCV) enters cells via interactions with several host factors, a key one being that between the viral E2 envelope glycoprotein and the CD81 receptor. We previously identified E2 tryptophan residue 420 (W420) as an essential CD81-binding residue. However, the importance of W420 in the context of the native virion is unknown, as those previous studies predate the infectious HCV cell culture (cell culture-derived HCV [HCVcc]) system. Here, we introduced four separate mutations (F, Y, A, or R) at position 420 within the infectious HCVcc JFH-1 genome and characterized thei

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