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Russian Chemical Reviews, 2005, Volume 74, Issue 1, Pages 61–76
DOI: https://doi.org/10.1070/RC2005v074n01ABEH001159
(Mi rcr384)
 

This article is cited in 19 scientific papers (total in 19 papers)

Catalytic sites of hydrolases: structures and catalytic cycles

S. D. Varfolomeev, I. A. Gariev, I. V. Uporov

Lomonosov Moscow State University, Faculty of Chemistry
Abstract: The applications of various bioinformatics methods and databases to the analysis and classification of proteins and search for active sites of enzymes are considered. The published data on the structures of active sites and mechanisms of action of hydrolases are analysed. It is emphasised that all of the known hydrolases can be divided into four groups according to the types of catalytic site which differ in the mechanisms of water activation. The mechanisms of water activation by catalytic groups in the active sites of hydrolases are discussed and the schemes of catalytic cycles characteristic of classical types of active sites of these enzymes are considered. Using glycosyl hydrolases and serine hydrolases as examples, it is demonstrated that different proteins possess common catalytic sites and mechanisms of action. The role of aspartic acid and histidine in the activation of hydrolase substrates and the role of structure-forming acids (glycine, proline, cysteine) in the structural organisation of the catalytic sites are considered.
Received: 09.08.2004
Bibliographic databases:
Document Type: Article
Language: English
Original paper language: Russian


Citation: S. D. Varfolomeev, I. A. Gariev, I. V. Uporov, “Catalytic sites of hydrolases: structures and catalytic cycles”, Usp. Khim., 74:1 (2005), 67–83; Russian Chem. Reviews, 74:1 (2005), 61–76
Linking options:
  • https://www.mathnet.ru/eng/rcr384
  • https://doi.org/10.1070/RC2005v074n01ABEH001159
  • https://www.mathnet.ru/eng/rcr/v74/i1/p67
  • This publication is cited in the following 19 articles:
    1. S. D. Varfolomeev, V. Švedas, E. N. Efremenko, A. M. Egorov, M. G. Khrenova, V. I. Tishkov, D. L. Atroshenko, A. A. Pometun, S. S. Savin, N. N. Ugarova, G. Yu. Lomakina, I. V. Gachok, I. V. Lyagin, V. I. Muronetz, A. P. Sinitsyn, O. A. Sinitsyna, A. M. Rojhkova, G. F. Makhaeva, S. O. Bachurin, O. I. Lavrik, D. O. Zharkov, A. V. Yudkina, O. M. Panasenko, A. A. Baykov, P. Masson, T. N. Pashirova, Z. M. Shaihutdinova, E. V. Popova, V. E. Tikhomirova, O. A. Kost, E. V. Kudryashova, N. V. Dobryakova, N. L. Klyachko, M. M. Veselov, A. V. Lopukhov, I. M. Le-Deygen, A. D. Usvaliev, I. V. Chudosai, N. L. Eremeev, M. E. Zvereva, M. Yu. Rubtsova, M. M. Ulyashova, G. V. Presnova, L. V. Sigolaeva, D. V. Pergushov, I. N. Kurochkin, E. G. Evtushenko, I. A. Boginskaya, Yu. Yu. Zvyagina, E. A. Slipchenko, O. V. Kryukova, M. V. Sedova, I. A. Ryzhikov, V. V. Shumyantseva, P. I. Koroleva, T. V. Bulko, L. E. Agafonova, R. A. Masamrekh, T. A. Filippova, A. V. Kuzikov, A. P. Savitsky, M. O. Shleeva, I. , Russian Chem. Reviews, 93:12 (2024), 1–55  mathnet  mathnet  crossref
    2. Anna M. Timofeeva, Sergey E. Sedykh, Tatyana A. Sedykh, Georgy A. Nevinsky, Vaccines, 11:9 (2023), 1494  crossref
    3. Kolchina N.V., Rychkov G.N., Kulminskaya A.A., Ibatullin F.M., Petukhov M.G., Bobrov K.S., Russ. J. Bioorg. Chem., 46:4 (2020), 563–571  crossref  isi  scopus
    4. Varfolomeev S.D. Lushchekina S.V. Nemukhin A.V., Her. Russ. Acad. Sci., 86:3 (2016), 185–192  crossref  isi  scopus
    5. Varfolomeev S.D. Lushchekina S.V. Nemukhin A.V. Kulakova A.M. Kots E.D. Makhaeva G.F. Delacour H. Lockridge O. Masson P., Russ. Chem. Bull., 65:6 (2016), 1592–1607  crossref  isi  scopus
    6. Michael Shokhen, Michal Hirsch, Netaly Khazanov, Rachel Ozeri, Nurit Perlman, Isr. J. Chem, 2014, n/a  crossref  isi
    7. Plínio Cunha Sathler, André Luiz Lourenço, Leonardo Alves Miceli, Carlos Rangel Rodrigues, Magaly Girão Albuquerque, Lúcio Mendes Cabral, Helena Carla Castro, Journal of Enzyme Inhibition and Medicinal Chemistry, 2013, 1  crossref  isi  scopus
    8. Mautusi Mitra, Sam Ng, Anastasios Melis, American J. of Biochemistry and Molecular Biology, 2:1 (2012), 1  crossref  scopus
    9. Demina O.V., Kononikhin A.S., Laptev A.V., Khodonov A.A., Nikolaev E.N., Varfolomeev S.D., Russ. Chem. Bull., 61:2 (2012), 422–441  crossref  isi  elib  scopus
    10. Nemukhin A.V., Grigorenko B.L., Lushchekina S.V., Varfolomeev S.D., Russ. Chem. Rev., 81:11 (2012), 1011–1025  mathnet  crossref  isi  elib  scopus
    11. S. V. Lushchekina, I. A. Kaliman, B. L. Grigorenko, A. V. Nemukhin, S. D. Varfolomeev, Russ Chem Bull, 60:11 (2011), 2196  crossref  isi  elib  scopus
    12. J. Dennis Pollack, Xueliang Pan, Dennis K. Pearl, Orig Life Evol Biosph, 2010  crossref  isi  scopus
    13. Antokhin A.M., Gainullina E.T., Taranchenko V.F., Ryzhikov S.B., Yavaeva D.K., Russ. Chem. Rev., 79:8 (2010), 713–727  mathnet  crossref  isi  elib  scopus
    14. Sergei Varfolomeev, Journal of Biotechnology, 136 (2008), S173  crossref  isi
    15. S. D. Varfolomeev, Kinet Catal, 48:4 (2007), 469  crossref  isi  elib  scopus
    16. O. M. Poltorak, E. S. Chukhrai, O. S. Pilipenko, L. F. Atyaksheva, A. E. Beregalov, Russ. J. Phys. Chem, 81:5 (2007), 808  crossref  isi  elib  scopus
    17. Varfolomeev S.D., Mendeleev Commun., 17:1 (2007), 7–9  crossref  isi  elib  scopus
    18. S. D. Varfolomeev, I. A. Gariev, I. V. Uporov, ChemInform, 36:28 (2005)  crossref
    19. Hrmova M., Streltsov V., Smith B., Vasella A., Varghese J., Fincher G., Biochemistry, 44:50 (2005), 16529–16539  crossref  isi  elib  scopus
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