| EC |
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, Gene, 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. |
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| [EC 3.4.11.3 created 1972] |
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