Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Enzyme Nomenclature. Recommendations 1992

Supplement 3 (1995)

Corrections and additions to EC 3.4 Peptidases

Prepared on behalf of the advisory panel on peptidase nomenclature by Alan J. Barrett, The Babraham Institute, Cambridge CB2 4AT, England

This supplement is as close as possible to the published version [see Eur. J. Biochem., 1996, 237, 1-5]. If you need to cite this supplement please quote this references as its source.

This document contains further additions and amendments to Enzyme Nomenclature (1992), published by Academic Press, Orlando, Florida. Supplement 1 and 2 were published in Eur. J. Biochem. 223, 1-5 (1994), and Eur. J. Biochem. 232, 1-6, 1995. The entries marked with an asterisk are revisions of the corresponding entries in Enzyme Nomenclature (1992). Families of peptidases are referred to by use of the numbering system of Rawlings, N.D. & Barrett, A.J. (Methods Enzymol. 244, 19-61 and 461-486, 1994; Methods Enzymol. 248, 105-120 and 183-228, 1995). Comments and suggestions on enzyme classification and nomenclature may be sent to Prof. K. F. Tipton, Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland.

Glossary

bleomycin an antibiotic (see [1])
captopril [2S]-1-(3-mercapto-2-methyl-propanoyl)-L-proline
globomycin an antibiotic (see [1])

References:

1. Bycroft, B.W. (ed.) (1987) Dictionary of antibiotics and related substances. Chapman and Hall, London

*3.4.11.6 Arginyl aminopeptidase

Reaction: Release of N-terminal Arg (and to a lesser extent Lys), preferentially from a dipeptide or a tripeptide

Other names: Arylamidase II; Arginine aminopeptidase; Aminopeptidase B; Cl--Activated arginine aminopeptidase; Cytosol aminopeptidase IV. See also Comments

Comments: Cytosolic enzyme from mammalian tissues, activated by Cl-. Possibly identical with leukotriene A4 hydrolase (EC 3.3.2.6) or bleomycin hydrolase, both of which show arginyl aminopeptidase activity [4,5]

References:

1. Hopsu, V.K., Mäkinen, K.K. & Glenner, G.G. (1966) Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: aminopeptidase B. Arch. Biochem. Biophys. 114, 557-566 and 567-575

2. Mäkinen, K.K., Mäkinen, P.-L. (1978) Purification and characterization of two human erythrocyte arylamidases preferentially hydrolysing N-terminal arginine and lysine residues. Biochem. J. 175, 1051-1067

3. Söderling, E. (1983) Substrate specifities of Cl--activated arginine aminopeptidases from human and rat origin. Arch. Biochem. Biophys. 220, 1-10

4. Nishimura, C., Suzuki, H., Tanaka, N. & Yamaguchi, H. (1989) Bleomycin hydrolase is a unique thiol aminopeptidase. Biochem. Biophys. Res. Commun. 163, 788-796

5. Orning, L., Gierse, J.K. & Fitzpatrick, F.A. (1994) The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity. J. Biol. Chem. 269, 11269-11273

*3.4.14.5 Dipeptidyl-peptidase IV

Reaction: Release of an N-terminal dipeptide, Xaa-XbbXcc-, from a polypeptide, preferentially when Xbb is Pro, provided Xcc is neither Pro nor hydroxyproline

Other Names: Dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; Postproline dipeptidyl aminopeptidase IV; Lymphocyte antigen CD26; Glycoprotein GP110

Comments: A homodimer. An integral protein of the plasma membrane of lymphocytes and other mammalian cells, in peptidase family S9. The reaction is similar to that of the unrelated X-Pro dipeptidyl-peptidase of lactococci

References:

1. Misumi, Y., Hayashi, Y., Arakawa, F. & Ikehara, Y. (1992) Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim. Biophys. Acta 1131, 333-336

2. David, F., Bernard, A.-M., Pierres, M. & Marguet, D. (1993) Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases. J .Biol. Chem. 268, 17247-17252

3. Ikehara, Y., Ogata, S. & Misumi, Y. (1994) Dipeptidyl-peptidase IV from rat liver. Methods Enzymol. 244, 215-227

3.4.14.11 X-Pro dipeptidyl-peptidase

Reaction: Hydrolyses Xaa-Pro bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Prop-nitroanilide and (sequentially) Tyr-ProPhe-ProGly-ProIle

Other names: X-Prolyl dipeptidyl aminopeptidase; PepX

Comments: The intracellular enzyme from Lactococcus lactis (190-kDa) is a member of peptidase family S15. The reaction is similar to that catalysed by dipeptidyl-peptidase IV of animals

References:

1. Zevaco, C., Monnet, V. & Gripon, J.-C. (1990) Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties. J. Appl. Bacteriol. 68, 357-366

2. Meyer-Barton, E.C., Klein, J.R., Imam, M. & Plapp, R. (1993) Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290. Appl. Microbiol. Biotechnol. 40, 82-89

3. Habibi-Najafi, M.B. & Lee, B.H. (1994) Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG. Appl. Microbiol. Biotechnol. 42, 280-286

4. Chich, J.-F., Gripon, J.-C. & Ribadeau-Dumas, B. (1995) Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents. Anal. Biochem. 224, 245-249

5. Chich, J.-F., Chapot-Chartier, M.P., Ribadeau-Dumas, B. & Gripon, J.-C. (1995) Identification of the active site serine of the X-prolyl aminopeptidase from Lactococcus lactis. FEBS Lett. 314, 139-142

*3.4.15.1 Peptidyl-dipeptidase A

Reaction: Release of a C-terminal dipeptide, oligopeptideXaa-Xbb, when Xaa is not Pro, and Xbb is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II

Other Names: Angiotensin I-converting enzyme; Kininase II; Dipeptidyl carboxypeptidase I; Peptidase P; Carboxycathepsin; Dipeptide hydrolase

Comments: A Cl--dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Member of peptidase family M2

References:

1. Soubrier, F., Alhenc-Gelas, F., Hubert, C., Allegrini, J., John, M., Tregear, G. & Corvol, P. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc. Natl. Acad. Sci. USA 85, 9386-9390

2. Ehlers, M.R.W., Fox, E.A., Strydom, D.J. & Riordan, J.F. (1989) Molecular cloning of human testicular angiotensin-converting enzyme: the testis enzyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. USA 86, 7741-7745

3. Wei, L., Clauser, E., Alhenc-Gelas, F. & Corvol, P. (1992) The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267, 13398-13405

4. Corvol, P., Williams, T.A. & Soubrier, F. (1995) Peptidyl dipeptidase A: angiotensin I-converting enzyme. Methods Enzymol. 248, 283-305

*[3.4.15.3 Transferred entry: now EC 3.4.15.5 - Peptidyl-dipeptidase Dcp]

3.4.15.5 Peptidyl-dipeptidase Dcp

Reaction: Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1' is Pro, or both P1 and P1' are Gly

Other names: Dipeptidyl carboxypeptidase

Comments: Known from E. coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3. Ac-AlaAla-Ala is a good test stubstrate [3]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and included in EC 3.4.15.1

References:

1. Yaron, A. (1976) Dipeptidyl carboxypeptidase from Escherichia coli. Methods Enzymol. 45, 599-610

2. Henrich, B., Becker, S., Schroeder, U. & Plapp, R. (1993) dcp Gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product. J. Bacteriol. 175, 7290-7300

3. Conlin, C.A. & Miller, C.G. (1995) Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella. Methods Enzymol. 248, 567-579

3.4.17.19 Carboxypeptidase Taq

Reaction: Release of a C-terminal amino acid with broad specificity, except for -Pro

Comments: A 56-kDa enzyme from Thermus aquaticus. Most active at 80° C. A member of peptidase family M32

References:

1. Lee, S.-H., Minagawa, E., Taguchi, H., Matsuzawa, H., Ohta, T., Kaminogawa, S. & Yamauchi, K. (1992) Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1. Biosci. Biotechnol. Biochem. 56, 1839-1844

2. Lee, S.-H., Taguchi, H., Yoshimura, E., Minagawa, E., Kaminogawa, S., Ohta, T. & Matsuzawa, H. (1994) Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli. Biosci. Biotechnol. Biochem. 58, 1490-1495

3.4.19.11 γ-D-Glutamyl-meso-diaminopimelate peptidase I

Reaction: Hydrolysis of γ-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-γ-D-Glu)-meso-A2pm and 7-(L-Ala-γ-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted

Other Names: Endopeptidase I

Comments: A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14. Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism [3]

References:

1. Arminjon, F., Guinand, M., Vacheron, M.-J. & Michel, G. (1977) Specificity profiles of the membrane-bound γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602. Eur. J. Biochem. 73, 557-565

2. Garnier, M., Vacheron, M.-J., Guinard, M. & Michel, G. (1985) Purification and partial characterization of the extracellular γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602. Eur. J. Biochem. 148, 539-543

3. Hourdou, M.-L., Guinand, M., Vacheron, M.-J., Michel, G., Denoroy, L., Duez, C., Englebert, S., Joris, B., Weber, G. & Ghuysen, J.-M. (1993) Characterization of the sporulation-related γ-D-glutamyl-(l)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein. Biochem. J. 292, 563-570

3.4.21.92 Endopeptidase Clp

Reaction: Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. α-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-TyrNHMec; and Leu-Tyr-LeuTyr-Trp, in which cleavage of the -TyrLeu- and -TyrTrp bonds also occurs)

Other Names: Endopeptidase Ti; Caseinolytic protease

Comments: An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2 [4]. ClpP is a member of peptidase family S14

References:

1. Gottesman, S., Clark, W.P. & Maurizi, M.R. (1990) The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J. Biol. Chem. 265, 7886-7893

2. Maurizi, M.R., Clark, W.P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B. & Gottesman, S. (1990) Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265, 12536-12545

3. Maurizi, M.R., Thompson, M.W., Singh, S.K. & Kim, S.-H. (1994) Endopeptidase Clp: the ATP-dependent Clp protease from Escherichia coli. Methods Enzymol. 244, 314-331

4. Kessell, M., Maurizi,M.R., Kim, B., Kocsis, E., Trus, B., Singh, S.K. & Steven, A.C. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250, 587-594

3.4.21.93 Proprotein convertase 1

Reaction: Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg bonds

Other Names: Prohormone convertase 3; Neuroendocrine convertase 1

Comments: A Ca2+-dependent enzyme, maximally active at about pH 5.5. Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. Unlike prohormone convertase 2, does not hydrolyse proluteinizing-hormone-releasing-hormone. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 2. A member of peptidase family S8

References:

1. Seidah, N.G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M. & Chrétien, M. (1990) cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol. 9, 415-424

2. Smeekens, S.P., Avruch, A.S., LaMendola, J., Chan, S.J. & Steiner, D.F. (1991) Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans. Proc. Natl. Acad. Sci. USA 88, 340-344

3. Steiner, D.F., Smeekens, S.P., Ohagi, S. & Chan, S.J. (1992) The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267, 23435-23438

4. Seidah, N.G. & Chrétien, M. (1994) Pro-protein convertases of the subtilisin/kexin family. Methods Enzymol. 244, 175-188

5. Jean, F., Basak, A., Dimaio, J., Seidah, N.G. & Lazure, C. (1995) An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor. Biochem. J. 307, 689-695

3.4.21.94 Proprotein convertase 2

Reaction: Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg bonds

Other Names: Neuroendocrine convertase 2

Comments: A Ca2+-dependent enzyme, maximally active at about pH 5.5. Specificity is broader than that of prohormone convertase 1. Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proglucagon, proinsulin and proluteinizing-hormone-releasing-hormone. Does not hydrolyse prorenin or prosomatostatin, however. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 1. A member of peptidase family S8

References:

1. Seidah, N.G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M. & Chrétien, M. (1990) cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases. DNA Cell Biol. 9, 415-424

2. Smeekens, S.P. & Steiner, D.F. (1990) Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem. 265, 2997-3000

3. Rouillé, Y., Westermark, G., Martin, S.K. & Steiner, D.F. (1994) Proglucagon is processed to glucagon by prohormone convertase PC2 in αTC1-6 cells. Proc. Natl. Acad. Sci. USA 91, 3242-3246

4. Seidah, N.G. & Chrétien, M. (1994) Pro-protein convertases of the subtilisin/kexin family. Methods Enzymol. 244, 175-188

*[3.4.22.11 Transferred entry: now EC 3.4.24.56 - Insulysin]

3.4.22.37 Gingipain R

Reaction: Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1

Other names: Arg-gingipain; Gingipain-1; Argingipain

Comments: A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine [1], and stabilized by Ca2+. Precursor molecule contains a haemagglutinin domain [2,3]. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase in family C25

References:

1. Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M. & Travis, J. (1992) Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J. Biol. Chem. 267, 18896-18901

2. Kirszbaum, L., Sotiropoulos, C., Jackson, C., Cleal, S., Slakeski, N. & Reynolds, E.C. (1995) Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain. Biochem. Biophys. Res. Commun. 207, 424-431.

3. Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. & Barr, P.J. (1995) Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein. J. Biol. Chem. 270, 1007-1010

3.4.24.70 Oligopeptidase A

Reaction: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-GlyGly-Pro-Ala is cleaved, but not Z-(Gly)5 [4]

Comments: Known from E. coli and Salmonella typhimurium. A zinc metallopeptidase, in peptidase family M3, but differs from thimet oligopeptidase in lack of thiol-activation

References:

1. Novak, P. & Dev, I.K. (1988) Degradation of a signal peptide by protease IV and oligopeptidase A. J. Bacteriol. 170, 5067-5075

2. Conlin, C.A., Vimr, E.R. & Miller, C.G. (1992) Oligopeptidase A is required for normal phage P22 development. J. Bacteriol. 174, 5869-5880

3. Conlin, C.A., Trun, N.J., Silhavy, T.J. & Miller, C.G. (1992) Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene. J. Bacteriol. 174, 5881-5887

4. Conlin, C.A. & Miller, C.G. (1995) Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella. Methods Enzymol. 248, 567-579

3.4.24.71 Endothelin-converting enzyme 1

Reaction: Hydrolysis of the -Trp21Val- bond in big endothelin to form endothelin 1

Comments: A phosphoramidon-sensitive metalloendopeptidase in peptidase family M13. An integral membrane protein predominantly of endothelial cells, which generates the potent vasoconstrictor endothelin 1 from its inactive precursor

References:

1. Takahashi, M., Matsushita, Y., Iijima, Y. & Tanzawa, K. (1993) Purification and characterization of endothelin-converting enzyme from rat lung. J. Biol. Chem. 268, 21394-21398

2. Shimada, K., Takahashi, M. & Tanzawa, K. (1994) Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J. Biol. Chem. 269, 18275-18278

3. Xu, D., Emoto, N., Giaid, A., Slaughter, C., Kaw, S., DeWit, D. & Yanagisawa, M. (1994) ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 78, 473-485

3.4.24.72 Fibrolase

Reaction: Hydrolysis of -Ala14Leu- in insulin B chain and -Lys413Leu- in Aα-chain of fibrinogen

Other Names: Fibrinolytic proteinase

Comments: A 23-kDa, non-haemorrhagic enzyme from the venom of the southern copperhead snake (Agkistrodon contortix contortix). Member of peptidase family M12

References:

1. Retzios, A.D. & Markland, F.S., Jr. (1988) A direct-acting fibrinolytic enzyme from the venom of Agkistrodon contortix contortix: effects on various components of the human blood coagulation and fibrinolysis systems. Thromb. Res. 52, 541-552

2. Guan, A.L., Retzios, A.D., Henderson, G.N. & Markland, F.S., Jr. (1991) Purification and characterization of a fibrinolytic enzyme from venom of southern copperhead snake (Agkistrodon contortrix contortrix). Arch. Biochem. Biophys. 289, 197-207

3. Randolph, A., Chamberlain, S.H., Chu, H.L.C., Retzios, A.D., Markland, F.S. Jr. & Masiarz, F.R. (1992) Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix venom. Protein Sci. 1, 590-600

4. Loayza, S.L., Trikha, M., Markland, F.S., Riquelme, P. & Kuo, J. (1994) Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrix snake venom, and comparison of their EDTA sensitivities. J. Chromatogr. B Biomed. Appl. 662, 227-243

5. Retzios, A.D. & Markland, F.S. (1994) Fibrinolytic enzymes from the venoms of Agkistrodon contortix contortix and Crotalus basilicus basilicus: cleavage site specificity towards the α-chain of fibrin. Thromb. Res. 74, 355-367

3.4.24.73 Jararhagin

Reaction: Hydrolysis of -His10Leu-, -Ala14Leu-, -Tyr16Leu- and -Phe24Phe- bonds in insulin B chain

Other Names: HF2-proteinase

Comments: Haemorrhagic endopeptidase from the venom of the jararaca snake (Bothrops jararaca). The 52-kDa enzyme contains a disintegrin domain [3]. A member of peptidase family M12

References:

1. Mandelbaum, F.R., Reichl, A.P. & Assakura, M.T. (1976) Some physical and biochemical characteristics of HF2, one of the hemorrhagic factors in the venom of Bothrops jararaca. In Animal, Plant and Microbial Toxins (Ohsaka, A., Hayashi, K. & Sawai, Y. eds), pp. 111-121, Plenum Press, New York

2. Assakura, M.T., Reichl, A.P. & Mandelbaum, F.R. (1986) Comparison of immunological, biochemical and biophysical properties of three hemorrhagic factors isolated from the venom of Bothrops jararaca (jararaca). Toxicon 24, 943-946

3. Paine, M.J.I., Desmond, H.P., Theakston, R.D.G. & Crampton, J.M. (1992) Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. J. Biol. Chem. 267, 22869-22876

*[3.4.99.10 Transferred entry: now EC 3.4.24.56 - Insulysin]


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