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Journal articles on the topic 'Zinc metalloenzyme'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Stoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (July 12, 1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.

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2

Vallee, B. L. "Zinc metalloenzyme structure and function." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 299. http://dx.doi.org/10.1016/0162-0134(89)84446-0.

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3

Haeggström, Jesper Z., Anders Wetterholm, Robert Shapiro, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: A zinc metalloenzyme." Biochemical and Biophysical Research Communications 172, no. 3 (November 1990): 965–70. http://dx.doi.org/10.1016/0006-291x(90)91540-9.

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4

Hadianawala, Murtuza, and Bhaskar Datta. "Design and development of sulfonylurea derivatives as zinc metalloenzyme modulators." RSC Advances 6, no. 11 (2016): 8923–29. http://dx.doi.org/10.1039/c5ra27341b.

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5

Millian, Norman S., and Timothy A. Garrow. "Human Betaine–Homocysteine Methyltransferase Is a Zinc Metalloenzyme." Archives of Biochemistry and Biophysics 356, no. 1 (August 1998): 93–98. http://dx.doi.org/10.1006/abbi.1998.0757.

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6

González, Julio C., Katrina Peariso, James E. Penner-Hahn, and Rowena G. Matthews. "Cobalamin-Independent Methionine Synthase fromEscherichia coli: A Zinc Metalloenzyme†." Biochemistry 35, no. 38 (January 1996): 12228–34. http://dx.doi.org/10.1021/bi9615452.

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7

Brothers, Edward N., Dimas Suarez, David W. Deerfield, and Kenneth M. Merz. "PM3-compatible zinc parameters optimized for metalloenzyme active sites." Journal of Computational Chemistry 25, no. 14 (2004): 1677–92. http://dx.doi.org/10.1002/jcc.20086.

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8

Tanaka, Tomoaki, and Eiji Ichishima. "Molecular properties of aminopeptidase ey as a zinc-metalloenzyme." International Journal of Biochemistry 25, no. 11 (November 1993): 1681–88. http://dx.doi.org/10.1016/0020-711x(93)90528-m.

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9

Shapir, Nir, Charlotte Pedersen, Omer Gil, Lisa Strong, Jennifer Seffernick, Michael J. Sadowsky, and Lawrence P. Wackett. "TrzN from Arthrobacter aurescens TC1 Is a Zinc Amidohydrolase." Journal of Bacteriology 188, no. 16 (August 15, 2006): 5859–64. http://dx.doi.org/10.1128/jb.00517-06.

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ABSTRACT TrzN, the broad-specificity triazine hydrolase from Arthrobacter and Nocardioides spp., is reportedly in the amidohydrolase superfamily of metalloenzymes, but previous studies suggested that a metal was not required for activity. To help resolve that conundrum, a double chaperone expression system was used to produce multimilligram quantities of functionally folded, recombinant TrzN. The TrzN obtained from Escherichia coli (trzN) cells cultured with increasing zinc in the growth medium showed corresponding increases in specific activity, and enzyme obtained from cells grown with 500 μ

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10

Álvarez-Santos, Silvia, Àngels González-Lafont, and José M. Lluch. "Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study." Canadian Journal of Chemistry 76, no. 7 (July 1, 1998): 1027–32. http://dx.doi.org/10.1139/v98-098.

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The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carb

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11

Khare, Sagar D., Yakov Kipnis, Per Jr Greisen, Ryo Takeuchi, Yacov Ashani, Moshe Goldsmith, Yifan Song, et al. "Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis." Nature Chemical Biology 8, no. 3 (February 5, 2012): 294–300. http://dx.doi.org/10.1038/nchembio.777.

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12

O’Young, Jason, Nicole Sukdeo, and John F. Honek. "Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme." Archives of Biochemistry and Biophysics 459, no. 1 (March 2007): 20–26. http://dx.doi.org/10.1016/j.abb.2006.11.024.

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13

PROUDFOOT, Amanda E. I., Laurence GOFFIN, Mark A. PAYTON, Timothy N. C. WELLS, and Alain R. BERNARD. "In vivo and in vitro folding of a recombinant metalloenzyme, phosphomannose isomerase." Biochemical Journal 318, no. 2 (September 1, 1996): 437–42. http://dx.doi.org/10.1042/bj3180437.

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Phosphomannose isomerase (PMI) catalyses the interconversion of mannose 6-phosphate and fructose 6-phosphate in prokaryotic and eukaryotic cells. The enzyme is a metalloenzyme which contains 1 mol of zinc per mol of enzyme. Heterologous expression of the cDNA coding for the Candida albicans enzyme in the prokaryotic host Escherichia coli results in an expression level of up to 30% of total E. coli protein. Ten percent of recombinant PMI is expressed in the soluble fraction and 90% in inclusion bodies. Inclusion of a high level of zinc in the fermentation medium resulted in a fourfold increase

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14

D’Ordine, Robert L., Rebecca S. Linger, Carolyn J. Thai, and V. Jo Davisson. "Catalytic Zinc Site and Mechanism of the Metalloenzyme PR-AMP Cyclohydrolase." Biochemistry 51, no. 29 (July 9, 2012): 5791–803. http://dx.doi.org/10.1021/bi300391m.

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15

Pettigrew, D. W., R. R. Bidigare, B. J. Mehta, M. I. Williams, and E. G. Sander. "Dihydro-orotase from Clostridium oroticum. Purification and reversible removal of essential zinc." Biochemical Journal 230, no. 1 (August 15, 1985): 101–8. http://dx.doi.org/10.1042/bj2300101.

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A new purification procedure involving five column-chromatography steps is described for dihydro-orotase (L-5,6-dihydro-orotate amidohydrolase, EC 3.5.2.3) from Clostridium oroticum (A.T.C.C. 25750). The native purified enzyme is a dimer of Mr 102 000 and contains 4.0 +/- 0.3 g-atoms of zinc/mol of dimer. These observations agree with those reported previously [Taylor, Taylor, Balch & Gilchrist (1976) J. Bacteriol. 127, 863-873]. It is conclusively demonstrated that dihydro-orotase is a zinc metalloenzyme. Zinc is reversibly removed by treatment with chelators in phosphate buffer at pH 6.5

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16

Komai, Michio, Tomoko Goto, Hitoshi Suzuki, Tomohiko Takeda, and Yuji Furukawa. "Zinc deficiency and taste dysfunction; Contribution of carbonic anhydrase, a zinc-metalloenzyme, to normal taste sensation." BioFactors 12, no. 1-4 (2000): 65–70. http://dx.doi.org/10.1002/biof.5520120111.

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17

May, Oliver, Martin Siemann, Michael G. Siemann, and Christoph Syldatk. "The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a zinc metalloenzyme." Journal of Molecular Catalysis B: Enzymatic 5, no. 1-4 (September 1998): 367–70. http://dx.doi.org/10.1016/s1381-1177(98)00060-5.

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18

Wetterholm, Anders, Juan F. Medina, Olof Rådmark, Robert Shapiro, Jesper Z. Haeggström, Bert L. Vallee, and Bengt Samuelsson. "Recombinant mouse leukotriene A4 hydrolase: a zinc metalloenzyme with dual enzymatic activities." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1080, no. 2 (October 1991): 96–102. http://dx.doi.org/10.1016/0167-4838(91)90134-l.

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19

Ruzicka, Frank J., Joseph E. Wedekind, Jeongmin Kim, Ivan Rayment, and Perry A. Frey. "Galactose-1-phosphate Uridylyltransferase from Escherichia coli, a Zinc and Iron Metalloenzyme." Biochemistry 34, no. 16 (April 25, 1995): 5610–17. http://dx.doi.org/10.1021/bi00016a036.

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20

Ohno, H., K. Yamashita, R. Doi, K. Yamamura, T. Kondo, and N. Taniguchi. "Exercise-induced changes in blood zinc and related proteins in humans." Journal of Applied Physiology 58, no. 5 (May 1, 1985): 1453–58. http://dx.doi.org/10.1152/jappl.1985.58.5.1453.

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Effects of cycle ergometer exercise (approximately 75% maximum ventilatory O2 consumption for 30 min) on the concentrations of zinc and related proteins in erythrocytes and/or plasma were studied on 11 sedentary male students. Lower concentrations of total zinc and of zinc derived from carbonic anhydrase I type (CA-I) in erythrocytes were observed immediately after exercise, but they disappeared after 30 min of rest. The change in total zinc concentration in erythrocytes correlated well with that in CA-I concentration immediately after exercise, as well as after rest. The concentration of carb

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21

Robinson, Sophia G., Philip T. Burns, Amanda M. Miceli, Kyle A. Grice, Caitlin E. Karver, and Lihua Jin. "Calorimetric studies of the interactions of metalloenzyme active site mimetics with zinc-binding inhibitors." Dalton Transactions 45, no. 29 (2016): 11817–29. http://dx.doi.org/10.1039/c6dt01675h.

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The binding of drugs to metalloenzymes is an intricate process that involves several interactions, including binding of the drug to the enzyme active site metal, as well as multiple interactions between the drug and the enzyme residues.

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22

Tsuchiya, Hironori. "Gustatory and Saliva Secretory Dysfunctions in COVID-19 Patients with Zinc Deficiency." Life 12, no. 3 (February 28, 2022): 353. http://dx.doi.org/10.3390/life12030353.

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Given the ever-progressing studies on coronavirus disease 2019 (COVID-19), it is critical to update our knowledge about COVID-19 symptomatology and pathophysiology. In the present narrative review, oral symptoms were overviewed using the latest data and their pathogenesis was hypothetically speculated. PubMed, LitCovid, ProQuest, and Google Scholar were searched for relevant studies from 1 April 2021 with a cutoff date of 31 January 2022. The literature search indicated that gustatory dysfunction and saliva secretory dysfunction are prevalent in COVID-19 patients and both dysfunctions persist

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23

Studer, Sabine, Douglas A. Hansen, Zbigniew L. Pianowski, Peer R. E. Mittl, Aaron Debon, Sharon L. Guffy, Bryan S. Der, Brian Kuhlman, and Donald Hilvert. "Evolution of a highly active and enantiospecific metalloenzyme from short peptides." Science 362, no. 6420 (December 13, 2018): 1285–88. http://dx.doi.org/10.1126/science.aau3744.

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Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency (kcat/KM~ 106M−1s−1). The simultaneous optimization o

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24

Jackman, Jane E., Christian R. H. Raetz, and Carol A. Fierke. "UDP-3-O-(R-3-Hydroxymyristoyl)-N-acetylglucosamine Deacetylase ofEscherichiacoliIs a Zinc Metalloenzyme†." Biochemistry 38, no. 6 (February 1999): 1902–11. http://dx.doi.org/10.1021/bi982339s.

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25

Beck, Jennifer L., Lyndal A. McConachie, Andrew C. Summors, Wilfred N. Arnold, John De Jersey, and Burt Zerner. "Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzyme." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 869, no. 1 (January 1986): 61–68. http://dx.doi.org/10.1016/0167-4838(86)90310-9.

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26

Temperini, Claudia, Alessio Innocenti, Andrea Scozzafava, and Claudiu T. Supuran. "N-Hydroxyurea—A versatile zinc binding function in the design of metalloenzyme inhibitors." Bioorganic & Medicinal Chemistry Letters 16, no. 16 (August 2006): 4316–20. http://dx.doi.org/10.1016/j.bmcl.2006.05.068.

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27

Jalilehvand, Farideh, Natalie Sisombath, Bonnie Leung, and Vicky Mah. "Silver(I) and Lead(II) Complex Formation with Thiolates." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C719. http://dx.doi.org/10.1107/s2053273314092808.

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Lead toxicity is frequently attributed to the displacement of essential metals such as zinc. Lead(II) ions mainly inhibit the enzymatic activity of ALAD, a key zinc-containing metalloenzyme in the heme biosynthetic pathway with much higher affinity to bind to Pb(II) than Zn(II) ions via its cysteinyl residues. Also for silver(I) ions the interaction with thiol-containing species such as cysteine and glutathione plays a key role in bacterial inactivation and Ag(I) antimicrobial activity. We will present the results of our investigations on Pb(II) and Ag(I) complex formation with small thiol-con

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28

Urbaniak, Michael D., Arthur Crossman, Tunhan Chang, Terry K. Smith, Daan M. F. van Aalten, and Michael A. J. Ferguson. "TheN-Acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of Glycosylphosphatidylinositol Biosynthesis Is a Zinc Metalloenzyme." Journal of Biological Chemistry 280, no. 24 (April 6, 2005): 22831–38. http://dx.doi.org/10.1074/jbc.m502402200.

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29

Patturajan, Meera, Mayalagu Sevugan, and Dipankar Chatterji. "DNA-Dependent RNA Polymerase II from Candida Species Is a Multiple Zinc-Containing Metalloenzyme." International Union of Biochemistry and Molecular Biology: Life 48, no. 2 (August 1, 1999): 163–68. http://dx.doi.org/10.1080/152165499307170.

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30

Patturajan, Meera, Mayalagu Sevugan, and Dipankar Chatterji. "DNA-Dependent RNA Polymerase II from Candida Species Is a Multiple Zinc-Containing Metalloenzyme." IUBMB Life 48, no. 2 (August 1, 1999): 163–68. http://dx.doi.org/10.1080/713803489.

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31

Sahin, H., R. Aliyazicioglu, O. Yildiz, S. Kolayli, A. Innocenti, and C. T. Supuran. "Honey, polen, and propolis extracts show potent inhibitory activity against the zinc metalloenzyme carbonic anhydrase." Journal of Enzyme Inhibition and Medicinal Chemistry 26, no. 3 (August 5, 2010): 440–44. http://dx.doi.org/10.3109/14756366.2010.503610.

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32

Giastas, Petros, Athena Andreou, Athanasios Papakyriakou, Dimitris Koutsioulis, Stavroula Balomenou, Socrates J. Tzartos, Vassilis Bouriotis, and Elias E. Eliopoulos. "Structures of the Peptidoglycan N-Acetylglucosamine Deacetylase Bc1974 and Its Complexes with Zinc Metalloenzyme Inhibitors." Biochemistry 57, no. 5 (January 5, 2018): 753–63. http://dx.doi.org/10.1021/acs.biochem.7b00919.

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33

Murphy, B. P., та R. F. Pratt. "A thiono-β-lactam substrate for the β-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate". Biochemical Journal 258, № 3 (15 березня 1989): 765–68. http://dx.doi.org/10.1042/bj2580765.

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An 8-thionocephalosporin was shown to be a substrate of the beta-lactamase II of Bacillus cereus, a zinc metalloenzyme. Although it is a poorer substrate, as judged by the Kcat./Km parameter, than the corresponding 8-oxocephalosporin, the discrimination against sulphur decreased when the bivalent metal ion in the enzyme active site was varied in the order Mn2+ (the manganese enzyme catalysed the hydrolysis of the oxo compound but not that of the thiono compound), Zn2+, Co2+ and Cd2+. This result is taken as evidence for kinetically significant direct contact between the active-site metal ion o

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34

Haeggström, Jesper Z., Pär Nordlund, and Marjolein M. G. M. Thunnissen. "Functional Properties and Molecular Architecture of Leukotriene A4 Hydrolase, a Pivotal Catalyst of Chemotactic Leukotriene Formation." Scientific World JOURNAL 2 (2002): 1734–49. http://dx.doi.org/10.1100/tsw.2002.810.

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The leukotrienes are a family of lipid mediators involved in inflammation and allergy. Leukotriene B4is a classical chemoattractant, which triggers adherence and aggregation of leukocytes to the endothelium at only nM concentrations. In addition, leukotriene B4modulates immune responses, participates in the host defense against infections, and is a key mediator of PAF-induced lethal shock. Because of these powerful biological effects, leukotriene B4 is implicated in a variety of acute and chronic inflammatory diseases, e.g., nephritis, arthritis, dermatitis, and chronic obstructive pulmonary d

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35

Han, Jin-Suk, and Kazuhiko Ishikawa. "Active site of Zn2+-dependentsn-glycerol-1-phosphate dehydrogenase fromAeropyrum pernixK1." Archaea 1, no. 5 (2005): 311–17. http://dx.doi.org/10.1155/2005/257264.

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The enzymesn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) is key to the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. This enzyme catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate. To date, no information about the active site and catalytic mechanism of this enzyme has been reported. Using the sequence and structural information for glycerol dehydrogenase, we constructed six mutants (D144N, D144A, D191N, H271A, H287A and D191N/H271A) of Gro1PDH fromAero

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36

Reiss, Y., M. S. Brown, and J. L. Goldstein. "Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme." Journal of Biological Chemistry 267, no. 9 (March 1992): 6403–8. http://dx.doi.org/10.1016/s0021-9258(18)42709-3.

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37

Izrael-Zivkovic, Lidija, Gordana Gojgic-Cvijovic, and Ivanka Karadzic. "Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853." Journal of the Serbian Chemical Society 75, no. 8 (2010): 1041–52. http://dx.doi.org/10.2298/jsc100125088i.

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Enzymatic characteristics of a protease from medically important, referent strain of Pseudomonas aeruginosa ATCC 27853 were determined. According to SDS PAGE and gel filtration it was estimated that molecular mass of the purified enzyme was about 15 kDa. Other enzymatic properties were found to be: pH optimum 7.1, pH stability between pH 6.5 and pH 10; temperature optimum around 60?C while the enzyme was stable at 60?C for 30 min. The inhibition of the enzyme was observed with the metal chelators such as EDTA and 1,10- phenanthroline, suggesting that the protease is a metalloenzyme. Further mo

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38

Huwiler, Simona G., Claudia Löffler, Sebastian E. L. Anselmann, Hans-Joachim Stärk, Martin von Bergen, Jennifer Flechsler, Reinhard Rachel, and Matthias Boll. "One-megadalton metalloenzyme complex inGeobacter metallireducensinvolved in benzene ring reduction beyond the biological redox window." Proceedings of the National Academy of Sciences 116, no. 6 (January 23, 2019): 2259–64. http://dx.doi.org/10.1073/pnas.1819636116.

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Reversible biological electron transfer usually occurs between redox couples at standard redox potentials ranging from +0.8 to −0.5 V. Dearomatizing benzoyl-CoA reductases (BCRs), key enzymes of the globally relevant microbial degradation of aromatic compounds at anoxic sites, catalyze a biological Birch reduction beyond the negative limit of this redox window. The structurally characterized BamBC subunits of class II BCRs accomplish benzene ring reduction at an active-site tungsten cofactor; however, the mechanism and components involved in the energetic coupling of endergonic benzene ring re

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39

Selvaraj, Ramesh K. "387 Effect of trace minerals (25-hydroxycholecalciferol, Zinc and Manganese) supplementation on the immune responses of livestock." Journal of Animal Science 98, Supplement_4 (November 3, 2020): 169. http://dx.doi.org/10.1093/jas/skaa278.310.

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Abstract Micronutrients such as 25-hydroxycholecalciferol, zinc and manganese are included in livestock feed to achieve optimal growth and improved immune function. Vitamin D (cholecalciferol) modulates immune responses. The effect of Vitamin D on immune cells depends on the subtype of immune cells. Monocytes and macrophages constitutively express Vitamin D receptor and hence 1, 25-dihydroxycholecalciferol increases maturation and the microbicidal activity of macrophages by increasing the production of nitric oxide, antimicrobial proteins and inflammatory cytokines and eventually acts to stimu

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40

Huang, Kai-Fa, Yi-Liang Liu, and Andrew H. J. Wang. "Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: A single zinc metalloenzyme." Protein Expression and Purification 43, no. 1 (September 2005): 65–72. http://dx.doi.org/10.1016/j.pep.2005.02.020.

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41

Krosky, Daniel J., Richard Alm, Mikael Berg, Gilles Carmel, Peter J. Tummino, Bo Xu, and Wei Yang. "Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1594, no. 2 (February 2002): 297–306. http://dx.doi.org/10.1016/s0167-4838(01)00319-3.

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42

Singh, Manoj Kumar, Zhen T. Chu, and Arieh Warshel. "Simulating the Catalytic Effect of a Designed Mononuclear Zinc Metalloenzyme that Catalyzes the Hydrolysis of Phosphate Triesters." Journal of Physical Chemistry B 118, no. 42 (October 13, 2014): 12146–52. http://dx.doi.org/10.1021/jp507592g.

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43

Basbous, Jihane, Antoine Aze, Laurent Chaloin, Rana Lebdy, Dana Hodroj, Cyril Ribeyre, Marion Larroque, et al. "Dihydropyrimidinase protects from DNA replication stress caused by cytotoxic metabolites." Nucleic Acids Research 48, no. 4 (December 19, 2019): 1886–904. http://dx.doi.org/10.1093/nar/gkz1162.

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Abstract Imbalance in the level of the pyrimidine degradation products dihydrouracil and dihydrothymine is associated with cellular transformation and cancer progression. Dihydropyrimidines are degraded by dihydropyrimidinase (DHP), a zinc metalloenzyme that is upregulated in solid tumors but not in the corresponding normal tissues. How dihydropyrimidine metabolites affect cellular phenotypes remains elusive. Here we show that the accumulation of dihydropyrimidines induces the formation of DNA–protein crosslinks (DPCs) and causes DNA replication and transcriptional stress. We used Xenopus egg

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44

Farsa, Oldřich, Veronika Ballayová, Radka Žáčková, Peter Kollar, Tereza Kauerová, and Peter Zubáč. "Aminopeptidase N Inhibitors as Pointers for Overcoming Antitumor Treatment Resistance." International Journal of Molecular Sciences 23, no. 17 (August 29, 2022): 9813. http://dx.doi.org/10.3390/ijms23179813.

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Aminopeptidase N (APN), also known as CD13 antigen or membrane alanyl aminopeptidase, belongs to the M1 family of the MA clan of zinc metallopeptidases. In cancer cells, the inhibition of aminopeptidases including APN causes the phenomenon termed the amino acid deprivation response (AADR), a stress response characterized by the upregulation of amino acid transporters and synthetic enzymes and activation of stress-related pathways such as nuclear factor kB (NFkB) and other pro-apoptotic regulators, which leads to cancer cell death by apoptosis. Recently, APN inhibition has been shown to augment

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45

Kim, Jin Kyun, Carrie L. Lomelino, Balendu Sankara Avvaru, Brian P. Mahon, Robert McKenna, SangYoun Park, and Chae Un Kim. "Active-site solvent replenishment observed during human carbonic anhydrase II catalysis." IUCrJ 5, no. 1 (January 1, 2018): 93–102. http://dx.doi.org/10.1107/s2052252517017626.

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Human carbonic anhydrase II (hCA II) is a zinc metalloenzyme that catalyzes the reversible hydration/dehydration of CO2/HCO3 −. Although hCA II has been extensively studied to investigate the proton-transfer process that occurs in the active site, its underlying mechanism is still not fully understood. Here, ultrahigh-resolution crystallographic structures of hCA II cryocooled under CO2 pressures of 7.0 and 2.5 atm are presented. The structures reveal new intermediate solvent states of hCA II that provide crystallographic snapshots during the restoration of the proton-transfer water network in

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46

Nishimura, Atsuhisa, Hiroshi Oyama, Takatoshi Hamada, Katsunori Nobuoka, Takashi Shin, Sawao Murao, and Kohei Oda. "Molecular Cloning, Sequencing, and Expression inEscherichia coli of the Gene Encoding a Novel 5-Oxoprolinase without ATP-Hydrolyzing Activity from Alcaligenes faecalis N-38A." Applied and Environmental Microbiology 66, no. 8 (August 1, 2000): 3201–5. http://dx.doi.org/10.1128/aem.66.8.3201-3205.2000.

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ABSTRACT The gene encoding a novel 5-oxoprolinase without ATP-hydrolyzing activity from Alcaligenes faecalis N-38A was cloned and characterized. The coding region of this gene is 1,299 bp long. The predicted primary protein is composed of 433 amino acid residues, with a 31-amino-acid signal peptide. The mature protein is composed of 402 amino acid residues with a molecular mass of 46,163 Da. The derived amino acid sequence of the enzyme showed no significant sequence similarity to any other proteins reported so far. The 5-oxoprolinase gene was expressed in Escherichia coli by using a regulator

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Mulrooney, Scott B., and Robert P. Hausinger. "Metal Ion Dependence of Recombinant Escherichia coli Allantoinase." Journal of Bacteriology 185, no. 1 (January 1, 2003): 126–34. http://dx.doi.org/10.1128/jb.185.1.126-134.2003.

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ABSTRACT Allantoinase is a suspected dinuclear metalloenzyme that catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid. Recombinant Escherichia coli allantoinase purified from overproducing cultures amended with 2.5 mM zinc, 1 mM cobalt, or 1 mM nickel ions was found to possess ∼1.4 Zn, 0.0 Co, 0.0 Ni, and 0.4 Fe; 0.1 Zn, 1.0 Co, 0.0 Ni, and 0.2 Fe; and 0.0 Zn, 0.0 Co, 0.6 Ni, and 0.1 Fe per subunit, respectively, whereas protein obtained from nonamended cultures contains near stoichiometric levels of iron. We conclude that allantoin

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Toyoshima, Manabu, Xuguang Jiang, Tadayuki Ogawa, Tetsuo Ohnishi, Shogo Yoshihara, Shabeesh Balan, Takeo Yoshikawa, and Nobutaka Hirokawa. "Enhanced carbonyl stress induces irreversible multimerization of CRMP2 in schizophrenia pathogenesis." Life Science Alliance 2, no. 5 (October 2019): e201900478. http://dx.doi.org/10.26508/lsa.201900478.

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Enhanced carbonyl stress underlies a subset of schizophrenia, but its causal effects remain elusive. Here, we elucidated the molecular mechanism underlying the effects of carbonyl stress in iPS cells in which the gene encoding zinc metalloenzyme glyoxalase I (GLO1), a crucial enzyme for the clearance of carbonyl stress, was disrupted. The iPS cells exhibited significant cellular and developmental deficits, and hyper-carbonylation of collapsing response mediator protein 2 (CRMP2). Structural and biochemical analyses revealed an array of multiple carbonylation sites in the functional motifs of C

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Kalinin, Stanislav, Anna Malkova, Tatiana Sharonova, Vladimir Sharoyko, Alexander Bunev, Claudiu T. Supuran, and Mikhail Krasavin. "Carbonic Anhydrase IX Inhibitors as Candidates for Combination Therapy of Solid Tumors." International Journal of Molecular Sciences 22, no. 24 (December 14, 2021): 13405. http://dx.doi.org/10.3390/ijms222413405.

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Combination therapy is becoming imperative for the treatment of many cancers, as it provides a higher chance of avoiding drug resistance and tumor recurrence. Among the resistance-conferring factors, the tumor microenvironment plays a major role, and therefore, represents a viable target for adjuvant therapeutic agents. Thus, hypoxia and extracellular acidosis are known to select for the most aggressive and resilient phenotypes and build poorly responsive regions of the tumor mass. Carbonic anhydrase (CA, EC 4.2.1.1) IX isoform is a surficial zinc metalloenzyme that is proven to play a central

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Holt, Jason A., Edward P. Garvey, J. David Becherer, William J. Hoekstra, Robert J. Schotzinger, and Christopher M. Yates. "SE-7552, a Highly Selective, Non-Hydroxamate Inhibitor of Histone Deacetylase-6 Blocks Multiple Myeloma Growth In Vivo." Blood 132, Supplement 1 (November 29, 2018): 3215. http://dx.doi.org/10.1182/blood-2018-99-113066.

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Abstract Despite recent advances, disease progression and treatment resistance in multiple myeloma (MM) remains a significant challenge. Current therapies include proteasome inhibitors, immunomodulatory agents, monoclonal antibodies and more recently histone deacetylase (HDAC) inhibitors. Many HDAC inhibitors have progressed into clinical development, however, there has been limited success with the approval of only three pan-HDAC inhibitors (SAHA, belinostat and panobinostat) and the class I selective inhibitor, romidepsin. A challenge to the development of HDAC inhibitors has been the manage

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