ExplorEnz: EC 3.4.*

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3.4.1.1

Transferred entry:

leucyl aminopeptidase. Now EC 3.4.11.1, leucyl aminopeptidase

[EC 3.4.1.1 created 1961, deleted 1972]

3.4.1.2

Transferred entry:

aminopeptidase. Now EC 3.4.11.2, membrane alanyl aminopeptidase

[EC 3.4.1.2 created 1961, deleted 1972]

3.4.1.3

Transferred entry:

aminotripeptidase. Now EC 3.4.11.4, tripeptide aminopeptidase

[EC 3.4.1.3 created 1961, deleted 1972]

3.4.1.4

Transferred entry:

proline iminopeptidase. Now EC 3.4.11.5, prolyl aminopeptidase

[EC 3.4.1.4 created 1965, deleted 1972]

3.4.2.1

Transferred entry:

carboxypeptidase A. Now EC 3.4.17.1, carboxypeptidase A

[EC 3.4.2.1 created 1961, deleted 1972]

3.4.2.2

Transferred entry:

carboxypeptidase B. Now EC 3.4.17.2, carboxypeptidase B

[EC 3.4.2.2 created 1961, deleted 1972]

3.4.2.3

Transferred entry:

yeast carboxypeptidase. Now EC 3.4.17.4, Gly-Xaa carboxypeptidase

[EC 3.4.2.3 created 1961, deleted 1972]

3.4.3.1

Transferred entry:

glycyl-glycine dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase

[EC 3.4.3.1 created 1961, deleted 1972]

3.4.3.2

Transferred entry:

glycyl-leucine dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase

[EC 3.4.3.2 created 1961, deleted 1972]

3.4.3.3

Transferred entry:

aminoacyl-histidine dipeptidase. Now EC 3.4.13.3, Xaa-His dipeptidase

[EC 3.4.3.3 created 1961, deleted 1972]

3.4.3.4

Transferred entry:

aminoacyl-methylhistidine dipeptidase. Now EC 3.4.13.5, Xaa-methyl-His dipeptidase

[EC 3.4.3.4 created 1961, deleted 1972]

3.4.3.5

Transferred entry:

cysteinylglycine dipeptidase. Now EC 3.4.11.2, membrane alanyl aminopeptidase

[EC 3.4.3.5 created 1961, deleted 1972]

3.4.3.6

Transferred entry:

iminodipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase

[EC 3.4.3.6 created 1961, deleted 1972]

3.4.3.7

Transferred entry:

iminodipeptidase. Now EC 3.4.13.9, Xaa-Pro dipeptidase

[EC 3.4.3.7 created 1961, deleted 1972]

3.4.4.1

Transferred entry:

pepsin. Now EC 3.4.23.1, pepsin A

[EC 3.4.4.1 created 1961, deleted 1972]

3.4.4.2

Transferred entry:

pepsin B. Now EC 3.4.23.2, pepsin B

[EC 3.4.4.2 created 1961, deleted 1972]

3.4.4.3

Transferred entry:

rennin. Now EC 3.4.23.4, chymosin

[EC 3.4.4.3 created 1961, deleted 1972]

3.4.4.4

Transferred entry:

trypsin. Now EC 3.4.21.4, trypsin

[EC 3.4.4.4 created 1961, deleted 1972]

3.4.4.5

Transferred entry:

chymotrypsin. Now EC 3.4.21.1, chymotrypsin

[EC 3.4.4.5 created 1961, deleted 1972]

3.4.4.6

Transferred entry:

chymotrypsin B. Now EC 3.4.21.1, chymotrypsin

[EC 3.4.4.6 created 1961, deleted 1972]

3.4.4.7

Transferred entry:

elastase. Now covered by EC 3.4.21.36, pancreatic elastase and EC 3.4.21.37, leukocyte elastase

[EC 3.4.4.7 created 1961, deleted 1972]

3.4.4.8

Transferred entry:

enteropeptidase. Now EC 3.4.21.9, enteropeptidase

[EC 3.4.4.8 created 1961, deleted 1972]

3.4.4.9

Transferred entry:

cathepsin C. Now EC 3.4.14.1, dipeptidyl-peptidase I

[EC 3.4.4.9 created 1961, deleted 1972]

3.4.4.10

Transferred entry:

papain. Now EC 3.4.22.2, papain

[EC 3.4.4.10 created 1961, deleted 1972]

3.4.4.11

Transferred entry:

chymopapain. Now EC 3.4.22.6, chymopapain

[EC 3.4.4.11 created 1961, deleted 1972]

3.4.4.12

Transferred entry:

ficin. Now EC 3.4.22.3, ficain

[EC 3.4.4.12 created 1961, deleted 1972]

3.4.4.13

Transferred entry:

thrombin. Now EC 3.4.21.5, thrombin

[EC 3.4.4.13 created 1961, deleted 1972]

3.4.4.14

Transferred entry:

plasmin. Now EC 3.4.21.7, plasmin

[EC 3.4.4.14 created 1961, deleted 1972]

3.4.4.15

Transferred entry:

renin. Now EC 3.4.23.15, renin

[EC 3.4.4.15 created 1961, deleted 1972]

3.4.4.16

Transferred entry:

subtilopeptidase A. Now covered by the microbial serine proteinases EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64 (endopeptidase K), EC 3.4.21.65 (thermomycolin), EC 3.4.21.66 (thermitase) and EC 3.4.21.67 (ndopeptidase So)

[EC 3.4.4.16 created 1961, deleted 1972]

3.4.4.17

Transferred entry:

aspergillopeptidase A. Now covered by the microbial aspartic proteinases EC 3.4.23.20 (penicillopepsin), EC 3.4.23.21 (rhizopuspepsin), EC 3.4.23.22 (endothiapepsin), EC 3.4.23.23 (mucorpepsin), EC 3.4.23.24 (candidapepsin), EC 3.4.23.25 (saccharopepsin), EC 3.4.23.26 (rhodotorulapepsin), EC 3.4.21.103 (physarolisin), EC 3.4.23.28 (acrocylindropepsin), EC 3.4.23.29 (polyporopepsin) and EC 3.4.23.30 (pycnoporopepsin)

[EC 3.4.4.17 created 1961, deleted 1972]

3.4.4.18

Transferred entry:

streptococcus peptidase A. Now EC 3.4.22.10, streptopain

[EC 3.4.4.18 created 1961, deleted 1972]

3.4.4.19

Transferred entry:

clostridiopeptidase A. Now EC 3.4.24.3, microbial collagenase

[EC 3.4.4.19 created 1961, deleted 1972]

3.4.4.20

Transferred entry:

clostridiopeptidase B. Now EC 3.4.22.8, clostripain

[EC 3.4.4.20 created 1961, deleted 1972]

3.4.4.21

Transferred entry:

kallikrein. Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein)

[EC 3.4.4.21 created 1965, deleted 1972]

3.4.4.22

Transferred entry:

now EC 3.4.23.3, gastricsin

[EC 3.4.4.22 created 1965, deleted 1972]

3.4.4.23

Transferred entry:

now EC 3.4.23.5, cathepsin D

[EC 3.4.4.23 created 1965, deleted 1972]

3.4.4.24

Transferred entry:

now covered by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain)

[EC 3.4.4.24 created 1965, deleted 1972]

3.4.4.25

Deleted entry:

Streptomyces alkalophilic keratinase

[EC 3.4.4.25 created 1965, deleted 1972]

3.4.11.1

Accepted name:

leucyl aminopeptidase

Reaction:

Release of an N-terminal amino acid, Xaa┼Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low

Other name(s):

leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I

Comments:

A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-61-0

References:

1.	Himmelhoch, S.R. Leucine aminopeptidase from swine kidney. Methods Enzymol. 19 (1970) 508–513.
2.	Delange, R.J. and Smith, E.L. Leucine aminopeptidase and other N-terminal exopeptidases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 3, Academic Press, New York, 1971, pp. 81–118.
3.	van Loon-Klaasen, L.A.H., Cuypers, H.T., van Westreenen, H., de Jong, W.W. and Bloemendal, H. The primary structure of bovine lens leucine aminopeptidase. Complete amino acid sequence of the N-terminal cyanogen bromide fragment and site limited tryptic digestion. Biochem. Biophys. Res. Commun. 95 (1980) 334–341. [DOI] [PMID: 7417261]

[EC 3.4.11.1 created 1961 as EC 3.4.1.1, transferred 1972 to EC 3.4.11.1]

3.4.11.2

Accepted name:

membrane alanyl aminopeptidase

Reaction:

Release of an N-terminal amino acid, Xaa┼Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide

Other name(s):

microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13

Comments:

A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9054-63-1

References:

1.	Wachsmuth, D., Fritze, I. and Pfleiderer, G. An aminopeptidase occurring in pig kidney. I. An improved method of preparation. Physical and enzymatic properties. Biochemistry 5 (1966) 169–174. [PMID: 5938934]
2.	Kim, Y.S. and Brophy, E.J. Rat intestinal brush border membrane peptidases. I. Solubilization, purification of two different forms of enzyme. J. Biol. Chem. 251 (1976) 3199–3205. [PMID: 931983]
3.	Gray, G.M. and Santiago, N.A. Intestinal surface amino-oligopeptidases. I. Isolation of two weight isomers and their subunits from rat brush border. J. Biol. Chem. 252 (1977) 4922–4928. [PMID: 873921]
4.	Sjöström, H., Norén, O., Jeppesen, L., Staun, M., Svensson, B. and Christiansen, L. Purification of different amphiphilic forms of a microvillus aminopeptidase from pig small intestine using immunoadsorbent chromatography. Eur. J. Biochem. 88 (1978) 503–511. [DOI] [PMID: 357150]
5.	Ferracci, H. and Maroux, S. Rabbit intestinal aminopeptidase N. Purification and molecular properties. Biochim. Biophys. Acta 599 (1980) 448–463. [DOI] [PMID: 6105876]

[EC 3.4.11.2 created 1961 as EC 3.4.1.2, transferred 1972 to EC 3.4.11.2 (EC 3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC 3.4.13.6, incorporated 1997)]

3.4.11.3

Accepted name:

cystinyl aminopeptidase

Reaction:

Release of an N-terminal amino acid, Cys┼Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however [4]

Other name(s):

cystyl-aminopeptidase; oxytocinase; cystine aminopeptidase; L-cystine aminopeptidase; oxytocin peptidase; vasopresssinase

Comments:

A zinc-containing sialoglycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-41-8

References:

1.	Sjöholm, I. Biochemical studies on oxytocin and oxytocinase. Acta Pharm. Suec. 4 (1967) 81–96. [PMID: 6041057]
2.	Sjöholm, I. and Yman, L. Degradation of oxytocin, lysine vasopressin, angiotensin II, and angiotensin II amide by oxytocinase (cystine aminopeptidase). Acta Pharm. Suec. 4 (1967) 65–76. [PMID: 4292447]
3.	Yman, L. Studies on human serum aminopeptidase. Some properties of oxytocinase, human serum aminopeptidase A and leucine aminopeptidase and their purification from retroplacental serum. Acta Pharm. Suec. 7 (1970) 75–86. [PMID: 5421622]
4.	Sakura, H., Lin, T.Y., Doi, M., Mizutani, S. and Kawashima, Y. Purification and properties of oxytocinase, a metalloenzyme. Biochem. Int. 2 (1981) 173–179.

[EC 3.4.11.3 created 1972]

3.4.11.4

Accepted name:

tripeptide aminopeptidase

Reaction:

Release of the N-terminal residue from a tripeptide

Other name(s):

tripeptidase; aminotripeptidase; aminoexotripeptidase; lymphopeptidase; imidoendopeptidase; peptidase B; alanine-phenylalanine-proline arylamidase; peptidase T

Comments:

A zinc enzyme, widely distributed in mammalian tissues. Formerly EC 3.4.1.3

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9056-26-2

References:

1.	Doumeng, C. and Maroux, S. Aminopeptidase, a cytosol enzyme from rabbit intestinal mucosa. Biochem. J. 177 (1979) 801–808. [PMID: 109082]
2.	Sachs, L. and Marks, N. A highly specific aminotripeptidase of rat brain cytosol. Substrate specifity and effects of inhibitors. Biochim. Biophys. Acta 706 (1982) 229–238. [DOI] [PMID: 7126601]

[EC 3.4.11.4 created 1961 as EC 3.4.1.3, transferred 1972 to EC 3.4.11.4]

3.4.11.5

Accepted name:

prolyl aminopeptidase

Reaction:

Release of N-terminal proline from a peptide

Other name(s):

proline aminopeptidase; Pro-X aminopeptidase; cytosol aminopeptidase V; proline iminopeptidase

Comments:

A Mn²⁺-requiring enzyme present in the cytosol of mammalian and microbial cells. In contrast to the mammalian form, the bacterial form of the enzyme (type example of peptidase family S33) hydrolyses both polyproline and prolyl-2-naphthylamide. The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1, leucyl aminopeptidase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-40-5

References:

1.	Sarid, S., Berger, A. and Katchalski, E. Proline iminopeptidase. II. Purification and comparison with iminopeptidase (prolinase). J. Biol. Chem. 237 (1962) 2207–2212. [PMID: 14497218]
2.	Nordwig, A. and Mayer, H. The cleavage of prolyl peptidases by kidney peptidases. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 380–383. [PMID: 4803482]
3.	Turzynski, A. and Mentlein, R. Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase. Eur. J. Biochem. 190 (1990) 509–515. [DOI] [PMID: 2373079]

[EC 3.4.11.5 created 1965 as EC 3.4.1.4, transferred 1972 to EC 3.4.11.5]

3.4.11.6

Accepted name:

aminopeptidase B

Reaction:

Release of N-terminal Arg and Lys from oligopeptides when P1′ is not Pro. Also acts on arylamides of Arg and Lys

Glossary:

amastatin = Leu[1Ψ²,CHOHCONH]ValValAsp
arphamenine A = Arg[1Ψ²,COCH2]Phe
arphamenine B = Arg[1Ψ²,COCH2]Tyr
bestatin = Phe[1Ψ²,CHOHCONH]Leu

Other name(s):

arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl^--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase

Comments:

Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family) [4,5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9073-92-1

References:

1.	Gainer, H., Russell, J.T. and Loh, Y.P. An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from β-lipotropin(60-65). FEBS Lett. 175 (1984) 135–139. [DOI] [PMID: 6434344]
2.	Belhacène, N., Mari, B., Rossi, B. and Auberger, P. Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation. Eur. J. Immunol. 23 (1993) 1948–1955. [DOI] [PMID: 8344358]
3.	Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D. and Cohen, P. Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules. Mol. Cell. Endocrinol. 110 (1995) 149–160. [PMID: 7672445]
4.	Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S. and Harada, M. Molecular cloning and expression of rat liver aminopeptidase B. J. Biol. Chem. 271 (1996) 30731–30735. [DOI] [PMID: 8940051]
5.	Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N. and Cohen, P. Aminopeptidase B from the rat testis is a bifunctional enzyme structually related to leukotriene-A₄ hydrolase. Proc. Natl. Acad. Sci. USA 94 (1997) 2963–2968. [DOI] [PMID: 9096329]
6.	Orning, L., Gierse, J.K. and Fitzpatrick, F.A. The bifunctional enzyme leukotriene-A₄ hydrolase is an arginine aminopeptidase of high efficiency and specificity. J. Biol. Chem. 269 (1994) 11269. [PMID: 8157657]

[EC 3.4.11.6 created 1972, modified 1997]

3.4.11.7

Accepted name:

glutamyl aminopeptidase

Reaction:

Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide

Other name(s):

aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca²⁺-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2

Comments:

Ca²⁺-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-83-3

References:

1.	Glenner, G.G., McMillan, P.J. and Folk, J.E. A mammalian peptidase specific for the hydrolysis of N-terminal α-L-glutamyl and aspartyl residues. Nature 194 (1962) 867. [PMID: 13899213]
2.	Chulkova, T.M. and Orekhovich, V.N. Isolation and properties of aminopeptidase A from bovine kidneys. Biokhimiya 43 (1978) 964–969. [PMID: 508862]
3.	Danielsen, E.M., Norén, O., Sjöström, H., Ingram, J. and Kenny, J. Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Biochem. J. 189 (1980) 591–603. [PMID: 7011318]
4.	Tobe, H., Kojima, F., Aoyagi, T. and Umezawa, H. Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney. Biochim. Biophys. Acta 613 (1980) 459–468. [DOI] [PMID: 7448199]
5.	Wu, Q., Lahti, J.M., Air, G.M., Burrows, P.D. and Cooper, M.D. Molecular cloning of the murine BP-1/6C3 antigen: a member of the zinc-dependent metallopeptidase family. Proc. Natl. Acad. Sci. USA 87 (1990) 993–997. [DOI] [PMID: 1689065]

[EC 3.4.11.7 created 1972]

3.4.11.8

Transferred entry:

pyroglutamyl aminopeptidase. Now EC 3.4.19.3, pyroglutamyl-peptidase I

[EC 3.4.11.8 created 1972, deleted 1981]

3.4.11.9

Accepted name:

Xaa-Pro aminopeptidase

Reaction:

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide

Other name(s):

proline aminopeptidase; aminopeptidase P; aminoacylproline aminopeptidase; X-Pro aminopeptidase

Comments:

A Mn²⁺-dependent, generally membrane-bound enzyme present in both mammalian and bacterial cells. In peptidase family M24 (methionyl aminopeptidase family)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37288-66-7

References:

1.	Yaron, A. and Mlynar, D. Aminopeptidase-P. Biochem. Biophys. Res. Commun. 32 (1968) 658–663. [DOI] [PMID: 4878817]
2.	Yaron, A. and Berger, A. Aminopeptidase-P. Methods Enzymol. 19 (1970) 522–534.
3.	Fleminger, G., Carmel, A. and Yaron, A. Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung. Eur. J. Biochem. 125 (1982) 609–615. [DOI] [PMID: 6749499]
4.	Orawski, A.T., Susz, J.P. and Simmons, W.H. Aminopeptidase-P from bovine lung - solubilization, properties, potential role in bradykinin degradation. Mol. Cell. Biochem. 75 (1987) 123–132. [PMID: 3627107]
5.	Hooper, N.M., Hryszko, J. and Turner, A.J. Purification and characterization of pig kidney aminopeptidase P. Biochem. J. 267 (1990) 509–515. [PMID: 2139778]

[EC 3.4.11.9 created 1972]

3.4.11.10

Accepted name:

bacterial leucyl aminopeptidase

Reaction:

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids

Other name(s):

Aeromonas proteolytica aminopeptidase

Comments:

A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Streptococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37288-67-8

References:

1.	Prescott, J.M. and Wilkes, S.H. Aeromonas aminopeptidase: purification and some general properties. Arch. Biochem. Biophys. 117 (1966) 328–336. [DOI] [PMID: 4961737]
2.	Dick, A.J., Matheson, A.T. and Wang, J.H. A ribosomal-bound aminopeptidase in Escherichia coli B: purification and properties. Can. J. Biochem. 48 (1970) 1181–1188. [PMID: 4920230]
3.	Rabier, D. and Desmazeaud, M.J. Inventaire des différentes activités peptidasiques intracellulaires de Streptococcus thermophilus. Purification et propriétés d’une dipeptide-hydrolase et d’une aminopeptidase. Biochimie 55 (1973) 389–404. [DOI] [PMID: 4749719]

[EC 3.4.11.10 created 1972]

3.4.11.11

Deleted entry:

aminopeptidase

[EC 3.4.11.11 created 1978, deleted 1992]