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Crystal structure of bovine duodenase, a serine protease, with dual trypsin and chymotrypsin-like specificities.

Pletnev VZ, Zamolodchikova TS, Pangborn WA, Duax WL
Proteins 41 8-16 (2000)
Cited: 21 times
EuropePMC logo PMID: 10944388

Abstract

The three-dimensional structure of duodenase, a serine protease from bovine duodenum mucosa, has been determined at 2.4A resolution. The enzyme, which has both trypsin-like and chymotrypsin-like activities, most closely resembles human cathepsin G with which it shares 57% sequence identity and similar specificity. The catalytic Ser195 in duodenase adopts the energetically favored conformation typical of serine proteinases and unlike the strained state typical of lipase/esterases. Of several waters in the active site of duodenase, the one associated with Ser214 is found in all serine proteinases and most lipase/esterases. The conservation of the Ser214 residue in serine proteinase, its presence in the active site, and participation in a hydrogen water network involving the catalytic triad (His57, Asp107, and Ser195) argues for its having an important role in the mechanism of action. It may be referred to as a fourth member of the catalytic triad. Duodenase is one of a growing family of enzymes that possesses trypsin-like and chymotrypsin-like activity. Not long ago, these activities were considered to be mutually exclusive. Computer modeling reveals that the S1 subsite of duodenase has structural features compatible with effective accommodation of P1 residues typical of trypsin (Arg/Lys) and chymotrypsin (Tyr/Phe) substrates. The determination of structural features associated with functional variation in the enzyme family may permit design of enzymes with a specific ratio of trypsin and chymotrypsin activities.

Articles - 1euf mentioned but not cited (2)

  1. Structural descriptor database: a new tool for sequence-based functional site prediction. Bernardes JS, Fernandez JH, Vasconcelos AT. BMC Bioinformatics 9 492 (2008)
  2. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. Ribeiro C, Togawa RC, Neshich IA, Mazoni I, Mancini AL, Minardi RC, da Silveira CH, Jardine JG, Santoro MM, Neshich G. BMC Struct. Biol. 10 36 (2010)


Reviews citing this publication (1)

  1. Serine proteases of small intestine mucosa--localization, functional properties, and physiological role. Zamolodchikova TS. Biochemistry Mosc. 77 820-829 (2012)

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  2. Molecular markers of serine protease evolution. Krem MM, Di Cera E. EMBO J. 20 3036-3045 (2001)
  3. Expansion of the mast cell chymase locus over the past 200 million years of mammalian evolution. Gallwitz M, Reimer JM, Hellman L. Immunogenetics 58 655-669 (2006)
  4. A despecialization step underlying evolution of a family of serine proteases. Wouters MA, Liu K, Riek P, Husain A. Mol. Cell 12 343-354 (2003)
  5. How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution. Raymond WW, Trivedi NN, Makarova A, Ray M, Craik CS, Caughey GH. J. Immunol. 185 5360-5368 (2010)
  6. Expression profile of novel members of the rat mast cell protease (rMCP)-2 and (rMCP)-8 families, and functional analyses of mouse mast cell protease (mMCP)-8. Gallwitz M, Enoksson M, Hellman L. Immunogenetics 59 391-405 (2007)
  7. Kinetics and thermodynamics of salt-dependent T7 gene 2.5 protein binding to single- and double-stranded DNA. Shokri L, Marintcheva B, Eldib M, Hanke A, Rouzina I, Williams MC. Nucleic Acids Res. 36 5668-5677 (2008)
  8. Defining the molecular forces that determine the impact of neomycin on bacterial protein synthesis: importance of the 2'-amino functionality. Barbieri CM, Kaul M, Bozza-Hingos M, Zhao F, Tor Y, Hermann T, Pilch DS. Antimicrob. Agents Chemother. 51 1760-1769 (2007)
  9. The extended substrate recognition profile of the dog mast cell chymase reveals similarities and differences to the human chymase. Gallwitz M, Enoksson M, Thorpe M, Ge X, Hellman L. Int. Immunol. 22 421-431 (2010)
  10. Cloning and molecular modeling of duodenase with respect to evolution of substrate specificity within mammalian serine proteases that have lost a conserved active-site disulfide bond. Zamolodchikova TS, Smirnova EV, Andrianov AN, Kashparov IV, Kotsareva OD, Sokolova EA, Ignatov KB, Pemberton AD. Biochemistry (Mosc) 70 672-684 (2005)
  11. Insights into the substrate specificity of a novel snake venom serine peptidase by molecular modeling. Vitorino-Cardoso AF, Pereira Ramos OH, Homsi-Brandeburgo MI, Selistre-de-Araujo HS. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 144 334-342 (2006)
  12. Murine serine proteases MASP-1 and MASP-3, components of the lectin pathway activation complex of complement, are encoded by a single structural gene. Stover CM, Lynch NJ, Dahl MR, Hanson S, Takahashi M, Frankenberger M, Ziegler-Heitbrock L, Eperon I, Thiel S, Schwaeble WJ. Genes Immun. 4 374-384 (2003)
  13. The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release. Thomas NE, Wu C, Morrison EA, Robinson AE, Werner JP, Henzler-Wildman KA. J. Biol. Chem. 293 19137-19147 (2018)
  14. [Duodenase activates rat peritoneal mast cells via protease-activated receptors of type 1] Makarova AM, Zamolodchikova TS, Rumsh LD, Strukova SM. Bioorg. Khim. 33 520-526 (2007)
  15. Cathepsin G-Not Only Inflammation: The Immune Protease Can Regulate Normal Physiological Processes. Zamolodchikova TS, Tolpygo SM, Svirshchevskaya EV. Front Immunol 11 411 (2020)
  16. Glutamyl Endopeptidases: The Puzzle of Substrate Specificity. Demidyuk IV, Chukhontseva KN, Kostrov SV. Acta Naturae 9 17-33 (2017)
  17. Interaction between human alpha2-macroglobulin and duodenase, a serine proteinase with dual specificity. Denisenko OO, Zamolodchikova TS, Popykina NA, Larionova NI. Biochemistry (Mosc) 71 658-666 (2006)
  18. Pancreatic proteolytic enzymes of ostrich purified on immobilized protein inhibitors. Characterization of a new form of chymotrypsin (Chtr1). Zelazko M, Chrzanowska J, Polanowski A. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 151 102-109 (2008)


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