The Enzyme Database

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EC 3.4.17.1     
Accepted name: carboxypeptidase A
Reaction: Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
Other name(s): carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A
Comments: A zinc enzyme formed from procarboxypeptidase A. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells [3] and skeletal muscle [4]. Type example of peptidase family M14.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 11075-17-5
References:
1.  Petra, P.H. Bovine procarboxypeptidase and carboxypeptidase A. Methods Enzymol. 19 (1970) 460–503.
2.  Reeck, G.R., Walsh, K.A. and Neurath, H. Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry 10 (1971) 4690–4698. [PMID: 5140186]
3.  Everitt, M.T. and Neurath, H. Rat peritoneal mast cell carboxypeptidase: localization, purification and enzymatic properties. FEBS Lett. 110 (1980) 292–296. [DOI] [PMID: 7371832]
4.  Bodwell, J.E. and Meyer, W.L. Purification and characterization of carboxypeptidase A from rat skeletal muscle. Biochemistry 20 (1981) 2767–2777. [PMID: 7018567]
[EC 3.4.17.1 created 1961 as EC 3.4.2.1, transferred 1972 to EC 3.4.12.2, transferred 1978 to EC 3.4.17.1]
 
 
EC 3.4.17.2     
Accepted name: carboxypeptidase B
Reaction: Preferential release of a C-terminal lysine or arginine amino acid
Other name(s): protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase
Comments: A zinc enzyme formed from procarboxypeptidase B. Isolated from cattle, pig and dogfish pancreas and other sources, including skin fibroblasts [3] and adrenal medulla [4]. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-24-5
References:
1.  Folk, J.E. Carboxypeptidase B (porcine pancreas). Methods Enzymol. 19 (1970) 504–508.
2.  Brodrick, J.W., Geokas, M.C. and Largman, C. Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion. Biochim. Biophys. Acta 452 (1976) 468–481. [DOI] [PMID: 1009123]
3.  Butterworth, J. and Duncan, J.J. Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis. Clin. Chim. Acta 97 (1979) 39–43. [DOI] [PMID: 40714]
4.  Wallace, E.F., Evans, C.J., Jurik, S.M., Mefford, I.N. and Barchas, J.D. Carboxypeptidase B activity from adrenal medulla. Is it involved in the processing of proenkephalin? Life Sci. 31 (1982) 1793–1796. [PMID: 6130442]
[EC 3.4.17.2 created 1961 as EC 3.4.2.2, transferred 1972 to EC 3.4.12.3, transferred 1978 to EC 3.4.17.2]
 
 
EC 3.4.17.3     
Accepted name: lysine carboxypeptidase
Reaction: Release of a C-terminal basic amino acid, preferentially lysine
Other name(s): carboxypeptidase N; arginine carboxypeptidase; kininase I; anaphylatoxin inactivator; plasma carboxypeptidase B; creatine kinase conversion factor; bradykinase; kininase Ia; hippuryllysine hydrolase; bradykinin-decomposing enzyme; protaminase; CPase N; creatinine kinase convertase; peptidyl-L-lysine(-L-arginine) hydrolase; CPN
Comments: A zinc enzyme found in plasma. Inactivates bradykinin and anaphylatoxins in blood plasma. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-89-2
References:
1.  Plummer, T.H., Jr. and Erdös, E.G. Human plasma carboxypeptidase N. Methods Enzymol. 80 (1981) 442–449. [PMID: 7341915]
2.  Levin, Y., Skidgel, R.A. and Erdös, E.G. Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I). Proc. Natl. Acad. Sci. USA 79 (1982) 4618–4622. [DOI] [PMID: 6750606]
3.  Skidgel, R.A. Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol. Sci. 9 (1988) 301–303. [DOI] [PMID: 3074547]
[EC 3.4.17.3 created 1972 as EC 3.4.12.7, transferred 1978 to EC 3.4.17.3, modified 1989]
 
 
EC 3.4.17.4     
Accepted name: Gly-Xaa carboxypeptidase
Reaction: Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly┼Leu
Other name(s): glycine carboxypeptidase; carboxypeptidase a; carboxypeptidase S; peptidase α; yeast carboxypeptidase; Gly-X carboxypeptidase
Comments: From yeast. In peptidase family M20 (glutamate carboxypeptidase family).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9025-25-6
References:
1.  Félix, F. and Brouillet, N. Purification et proprietes de deux peptidases de levure de brasserie. Biochim. Biophys. Acta 122 (1966) 127–144. [PMID: 4961236]
2.  Wolf, D.H. and Ehmann, C. Carboxypeptidase S from yeast: regulation of its activity during vegetative growth and differentiation. FEBS Lett. 91 (1978) 59–62. [DOI] [PMID: 352726]
[EC 3.4.17.4 created 1961 as EC 3.4.2.3, transferred 1972 to EC 3.4.12.8, transferred 1978 to EC 3.4.17.4 (EC 3.4.17.9 created 1981, incorporated 1992)]
 
 
EC 3.4.17.5      
Deleted entry: aspartate carboxypeptidase
[EC 3.4.17.5 created 1972 as EC 3.4.12.9, transferred 1978 to EC 3.4.17.5, deleted 1992]
 
 
EC 3.4.17.6     
Accepted name: alanine carboxypeptidase
Reaction: Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups
Other name(s): N-benzoyl-L-alanine-amidohydrolase
Comments: From soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-70-3
References:
1.  Levy, C.C. and Goldman, P. Bacterial peptidases. J. Biol. Chem. 244 (1969) 4467–4472. [PMID: 5806587]
2.  Miyagawa, E., Takahiro, H. and Yoshinobu, M. Purification and properties of N-benzoyl-L-alanine amidohydrolase from Corynebacterium equii. Agric. Biol. Chem. 50 (1986) 1527–1531.
[EC 3.4.17.6 created 1972 as EC 3.4.12.11, transferred 1978 to EC 3.4.17.6]
 
 
EC 3.4.17.7      
Transferred entry: acylmuramoyl-alanine carboxypeptidase. Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase
[EC 3.4.17.7 created 1978, deleted 1992]
 
 
EC 3.4.17.8     
Accepted name: muramoylpentapeptide carboxypeptidase
Reaction: Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanyl┼D-alanine
Other name(s): D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY
Comments: A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanine. Competitively inhibited by penicillins and cephalosporins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9077-67-2
References:
1.  Izaki, K. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J. Biol. Chem. 243 (1968) 3193–3201. [PMID: 4871206]
[EC 3.4.17.8 created 1972 as EC 3.4.12.6, transferred 1978 to EC 3.4.17.8]
 
 
EC 3.4.17.9      
Transferred entry: carboxypeptidase S. Now included with EC 3.4.17.4, Gly-Xaa carboxypeptidase
[EC 3.4.17.9 created 1981, deleted 1992]
 
 
EC 3.4.17.10     
Accepted name: carboxypeptidase E
Reaction: Release of C-terminal arginine or lysine residues from polypeptides
Other name(s): carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase
Comments: A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81876-95-1
References:
1.  Qian, Y.M., Varlamov, O. and Fricker, L.D. Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. J. Biol. Chem. 274 (1999) 11582–11586. [DOI] [PMID: 10206965]
2.  Fricker, L.D. Carboxypeptidase E/H. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1341–1344.
3.  Fricker, L.D. Methods for studying carboxypeptidase E. Methods Neurosci. 23 (1995) 237–250.
4.  Manser, E., Fernandez, D. , Loo,L., Goh, P.Y., Monfries, C., Hall, C. and Lim, L. Human carboxypeptidase E: isolation and characterisaton of the cDNA, sequence conservation, expression and processing in vitro. Biochem. J. 267 (1990) 517–525. [PMID: 2334405]
5.  Fricker, L.D. Carboxypeptidase E. Annu. Rev. Physiol. 50 (1988) 309–321. [DOI] [PMID: 2897826]
[EC 3.4.17.10 created 1986, modified 2000]
 
 
EC 3.4.17.11     
Accepted name: glutamate carboxypeptidase
Reaction: Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups
Other name(s): carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase
Comments: A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Goldman, P. and Levy, C.C. Carboxypeptidase G: purification and properties. Proc. Natl Acad. Sci. USA 58 (1967) 1299–1306. [DOI] [PMID: 5237864]
2.  McCullogh, J.L., Chabner, B.A. and Bertino, J.R. Purification and properties of carboxypeptidase G1. J. Biol. Chem. 246 (1971) 7207–7213. [PMID: 5129727]
3.  Albrecht, A.M., Boldizar, E. and Hutchinson, D.J. Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin. J. Bacteriol. 134 (1978) 506–513. [PMID: 26657]
4.  Sherwood, R.F., Melton, R.G. and Alwan, S.A. Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Eur. J. Biochem. 148 (1985) 447–453. [DOI] [PMID: 3838935]
[EC 3.4.17.11 created 1992]
 
 
EC 3.4.17.12     
Accepted name: carboxypeptidase M
Reaction: Cleavage of C-terminal arginine or lysine residues from polypeptides
Other name(s): CPM
Comments: A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 120038-28-0
References:
1.  Skidgel, R.A. Basic carboxypeptidases: Regulators of peptide hormone activity. Trends Pharmacol. Sci. 9 (1988) 303–304. [DOI] [PMID: 3074547]
2.  Deddish, P.A., Skidgel, R.A. and Erdös, E.G. Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Biochem. J. 261 (1989) 289–291. [PMID: 2775217]
3.  Skidgel, R.A., Davis, R.M. and Tan, F. Human carboxypeptidase M. Purification and characterization of membrane-bound carboxypeptidase that cleaves peptide hormones. J. Biol. Chem. 264 (1989) 2236–2241. [PMID: 2914904]
[EC 3.4.17.12 created 1992]
 
 
EC 3.4.17.13     
Accepted name: muramoyltetrapeptide carboxypeptidase
Reaction: Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl┼D-alanine
Other name(s): carboxypeptidase IIW; carboxypeptidase II; lysyl-D-alanine carboxypeptidase; L-lysyl-D-alanine carboxypeptidase; LD-carboxypeptidase
Comments: Variants are known from various microorganisms. Involved in peptidoglycan synthesis, catalysing both decarboxylation and transpeptidation. Stimulated by divalent cations such as Mg2+ and Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but unaffected by penicillin
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-80-1
References:
1.  DasGupta, H. and Fan, D.P. Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan. J. Biol. Chem. 254 (1979) 5672–5683. [PMID: 109439]
2.  Rousset, A., Nguyen-Disteche, M., Minck, R. and Ghuysen, J.-M. Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms. J. Bacteriol. 152 (1982) 1042–1048. [PMID: 6754695]
3.  Metz, R., Henning, S. and Hammes, W.P. LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12. Arch. Microbiol. 144 (1986) 181–186. [PMID: 3521530]
[EC 3.4.17.13 created 1992]
 
 
EC 3.4.17.14     
Accepted name: zinc D-Ala-D-Ala carboxypeptidase
Reaction: Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl┼D-alanine
Other name(s): Zn2+ G peptidase, D-alanyl-D-alanine hydrolase; D-alanyl-D-alanine-cleaving carboxypeptidase; DD-carboxypeptidase; G enzyme; DD-carboxypeptidase-transpeptidase
Comments: A zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Weakly inhibited by β-lactams. In peptidase family M15. Distinct from EC 3.4.16.4, serine-type D-Ala-D-Ala carboxypeptidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 213189-85-6
References:
1.  Dideberg, O., Charlier, P., Dive, G., Joris, B., Frère, J.M. and Ghuysen, J.M. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature 299 (1982) 469–470. [PMID: 7121588]
2.  Joris, B., Van Beeumen, J., Casagrande, F., Gerday, C., Frère, J.-M. and Ghuysen, J.-M. The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. Eur. J. Biochem. 130 (1983) 53–69. [DOI] [PMID: 6825689]
3.  Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J., Dusart, J., Joris, B., Duez, C., Dideberg, O., Charlier, P., Dive, G. and Lamotte-Brasseur, J. Bacterial wall peptidoglycan, DD-peptidases and β-lactam antibiotics. Scand. J. Infect. Dis. Suppl. 42 (1984) 17–37. [PMID: 6597561]
[EC 3.4.17.14 created 1992]
 
 
EC 3.4.17.15     
Accepted name: carboxypeptidase A2
Reaction: Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
Other name(s): CPA2
Comments: Isolated from rat pancreas but not present in cattle pancreas. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 181186-98-1
References:
1.  Gardell, S.J., Craik, C.S., Clauser, E., Goldsmith, E.J., Stewart, C.B., Graf, M. and Rutter, W.J. A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family. J. Biol. Chem. 263 (1988) 17828–17836. [PMID: 3182871]
[EC 3.4.17.15 created 1992]
 
 
EC 3.4.17.16     
Accepted name: membrane Pro-Xaa carboxypeptidase
Reaction: Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
Other name(s): carboxypeptidase P; microsomal carboxypeptidase; membrane Pro-X carboxypeptidase
Comments: One of the renal brush border exopeptidases
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-64-3
References:
1.  Dehm, P. and Nordwig, A. The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney. Eur. J. Biochem. 17 (1970) 372–377. [DOI] [PMID: 5500406]
2.  Booth, A.G., Hubbard, L.M.L. and Kenny, A.J. Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolase: identification and resolution of the detergent- and proteinase-solubilized forms. Biochem. J. 179 (1979) 397–405. [PMID: 486090]
3.  Hedeager-Sorensen, S. and Kenny, A.J. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys. Biochem. J. 229 (1985) 251–257. [PMID: 4038259]
[EC 3.4.17.16 created 1992]
 
 
EC 3.4.17.17     
Accepted name: tubulinyl-Tyr carboxypeptidase
Reaction: Cleavage of the -Glu┼Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr
Other name(s): carboxypeptidase-tubulin; soluble carboxypeptidase; tubulin-tyrosine carboxypeptidase; tubulin carboxypeptidase; tubulinyltyrosine carboxypeptidase; tyrosinotubulin carboxypeptidase; tyrosyltubulin carboxypeptidase; TTCPase; brain I carboxypeptidase
Comments: Active at neutral pH, from brain
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73050-23-4
References:
1.  Argaraña, C.E., Barra, H.S. and Caputto, R. Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification. J. Neurochem. 34 (1980) 114–118. [DOI] [PMID: 7452228]
2.  Kumar, N. and Flavin, M. Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin. J. Biol. Chem. 256 (1981) 7678–7686. [PMID: 6114100]
3.  Arce, C.A. and Barra, H.S. Association of tubulinyl-tyrosine carboxypeptidase with microtubules. FEBS Lett. 157 (1983) 75–78. [DOI] [PMID: 6862022]
[EC 3.4.17.17 created 1992]
 
 
EC 3.4.17.18     
Accepted name: carboxypeptidase T
Reaction: Releases a C-terminal residue, which may be hydrophobic or positively charged
Other name(s): CPT
Comments: Known from Thermoactinomyces vulgaris. In peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 89623-65-4
References:
1.  Osterman, A.L., Stepanov, V.M., Rudenskaya, G.N., Khodova, O.M., Tsaplina, I.A., Yakovleva, M.B. and Loginova, L.G. Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases. Biochemistry (USSR) 49 (1984) 292–301. [PMID: 6424730]
2.  Smulevitch, S.V., Osterman, A.L., Galperina, O.V., Matz, M.V., Zagnitko, O.P., Kadyrov, R.M., Tsaplina, I.A., Grishin, N.V., Chestukhina, G.G. and Stepanov, V.M. Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity. FEBS Lett. 291 (1991) 75–78. [DOI] [PMID: 1936254]
3.  Teplyakov, A., Polyakov, K., Obmolova, G., Strokopytov, B., Kuranova, I., Osterman, A., Grishin, N., Smulevitch, S., Zagnitko, O., Galperina, O., Matz, M. and Stepanov, V. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris. Eur. J. Biochem. 208 (1992) 281–288. [DOI] [PMID: 1521526]
[EC 3.4.17.18 created 1993]
 
 
EC 3.4.17.19     
Accepted name: 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. Type example of peptidase family M32
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-98-5
References:
1.  Lee, S.-H., Minagawa, E., Taguchi, H., Matsuzawa, H., Ohta, T., Kaminogawa, S. and Yamauchi, K. Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1. Biosci. Biotechnol. Biochem. 56 (1992) 1839–1844. [DOI] [PMID: 1369078]
2.  Lee, S.-H., Taguchi, H., Yoshimura, E., Minagawa, E., Kaminogawa, S., Ohta, T. and Matsuzawa, H. 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 (1994) 1490–1495. [DOI] [PMID: 7765282]
[EC 3.4.17.19 created 1996]
 
 
EC 3.4.17.20     
Accepted name: carboxypeptidase U
Reaction: Release of C-terminal Arg and Lys from a polypeptide
Other name(s): arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor
Comments: Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 156621-18-0
References:
1.  Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W. and Drayna, D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266 (1991) 21833–21838. [PMID: 1939207]
2.  Shinohara, T., Sakurada, C., Suzuki, T., Takeuchi, O., Campbell, W., Ikeda, S., Okada, N. and Okada, H. Pro-carboxypeptidase R cleaves bradykinin following activation. Int. Arch. Allergy Immunol. 103 (1994) 400–404. [DOI] [PMID: 8130654]
3.  Wang, W., Hendriks, D.F. and Scharpé, S. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J. Biol. Chem. 269 (1994) 15937–15944. [PMID: 8195249]
4.  Tan, A.K. and Eaton, D.L. Activation and characterization of procarboxypeptidase B from human plasma. Biochemistry 34 (1995) 5811–5816. [PMID: 7727441]
5.  Broze, G.J., Jr. and Higuchi, D.A. Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase U and the premature lysis of clots from hemophilic plasma. Blood 88 (1996) 3815–3823. [PMID: 8916945]
[EC 3.4.17.20 created 1997]
 
 
EC 3.4.17.21     
Accepted name: glutamate carboxypeptidase II
Reaction: Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-γ-glutamates
Glossary: quisqualic acid = 3-(3,5-dioxo-1,2,4-oxazadiazolidin-2-yl)Ala
Other name(s): N-acetylated-γ-linked-acidic dipeptidase (NAALADase); folate hydrolase; prostate-specific membrane antigen; pteroylpoly-γ-glutamate carboxypeptidase; microsomal γ-glutamyl carboxypeptidase; pteroylpolyglutamate hydrolase; folylpolyglutamate hydrolase; pteroylpoly-γ-glutamate hydrolase; pteroylpolyγglutamyl hydrolase; pteroylpolyglutamate hydrolase; pteroylpolyglutamic acid hydrolase; PSM antigen; acetylaspartylglutamate dipeptidase; NAALA dipeptidase; rat NAAG peptidase; mGCP; membrane glutamate carboxypeptidase; N-acetylated-α-linked-amino dipeptidase; prostrate-specific membrane antigen; N-Acetylated α-linked acidic dipeptidase; PSMA
Comments: A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa , but also exists in a soluble form. Hydrolyses α-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also γ-glutamyl bonds in γ-Glu-Glu, and folylpoly-γ-glutamates. With folylpoly-γ-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate [4]. Does not hydrolyse Ac-β-Asp-Glu. Known inhibitors: quisqualic acid, Ac-β-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. The release of C-terminal glutamate from folylpoly-γ-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (γ-Glu-X carboxypeptidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Heston, W.D.W. Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase. Urology 49 (1997) 104–112. [PMID: 9123729]
2.  Rawlings, N.D. and Barrett, A.J. Structure of membrane glutamate carboxypeptidase. Biochim. Biophys. Acta 1339 (1997) 247–252. [DOI] [PMID: 9187245]
3.  Halsted, C.H., Ling, E.-H., Luthi-Carter, R., Villanueva, J.A., Gardner, J.M., Coyle, J.T. Folylpoly-γ-glutamate carboxypeptidase from pig jejunum: molecular characterization and relation to glutamate carboxypeptidase II. J. Biol. Chem. 273 (1998) 20417–20424. [DOI] [PMID: 9685395]
4.  Luthi-Carter, R., Berger, U.V., Barczak, A.K., Enna, M. and Coyle, J.T. Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II. Proc. Natl. Acad. Sci. USA 95 (1998) 3215–3220. [DOI] [PMID: 9501243]
[EC 3.4.17.21 created 1997, modified 2000 (EC 3.4.13.8 created 1972 and EC 3.4.19.8 created 1992, incorporated 2000)]
 
 
EC 3.4.17.22     
Accepted name: metallocarboxypeptidase D
Reaction: Releases C-terminal Arg and Lys from polypeptides
Other name(s): carboxypeptidase D (cattle, human, mouse, rat); gp180 (duck)
Comments: Activated by Co2+; inhibited by guanidinoethylmercaptosuccinic acid. Large molecule (180 kDa) because of presence of three copies of metallopeptidase domain. The product of the silver gene (Drosophila) is similar. A zinc metallopeptidase in peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 153967-26-1
References:
1.  Kuroki, K., Eng, F., Ishikawa, T., Turck, C., Harada, F. and Ganem, D. gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J. Biol. Chem. 270 (1995) 15022–15028. [DOI] [PMID: 9525948]
2.  Song, L.X. and Fricker, L.D. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem. 270 (1995) 25007–25013. [DOI] [PMID: 7559630]
3.  Song, L.X. and Fricker, L.D. Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J. Biol. Chem. 271 (1996) 28884–28889. [DOI] [PMID: 8910535]
[EC 3.4.17.22 created 1997]
 
 
EC 3.4.17.23     
Accepted name: angiotensin-converting enzyme 2
Reaction: angiotensin II + H2O = angiotensin-(1–7) + L-phenylalanine
Other name(s): ACE-2; ACE2; hACE2; angiotensin converting enzyme 2; angiotensin converting enzyme-2; Tmem27
Comments: A transmembrane glycoprotein with an extracellular catalytic domain. Angiotensin-converting enzyme 2 functions as a carboxypeptidase, cleaving a single C-terminal residue from a distinct range of substrates [2]. Catalytic efficiency is 400-fold higher with angiotensin II (1–8) as a substrate than with angiotensin I (1–10). Angiotensin-converting enzyme 2 also efficiently hydrolyses des-Arg9-bradykinin, but it does not hydrolyse bradykinin [1]. In peptidase family M2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS
References:
1.  Vickers, C., Hales, P., Kaushik, V., Dick, L., Gavin, J., Tang, J., Godbout, K., Parsons, T., Baronas, E., Hsieh, F., Acton, S., Patane, M., Nichols, A. and Tummino, P. Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. J. Biol. Chem. 277 (2002) 14838–14843. [DOI] [PMID: 11815627]
2.  Lambert, D.W., Hooper, N.M. and Turner, A.J. Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system. Biochem. Pharmacol. 75 (2008) 781–786. [DOI] [PMID: 17897633]
3.  Towler, P., Staker, B., Prasad, S.G., Menon, S., Tang, J., Parsons, T., Ryan, D., Fisher, M., Williams, D., Dales, N.A., Patane, M.A. and Pantoliano, M.W. ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J. Biol. Chem. 279 (2004) 17996–18007. [DOI] [PMID: 14754895]
[EC 3.4.17.23 created 2009]
 
 


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