Peptidyl-glycinamidase |
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Identifiers |
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EC no. | 3.4.19.2 |
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CAS no. | 94047-14-0 |
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Databases |
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IntEnz | IntEnz view |
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BRENDA | BRENDA entry |
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ExPASy | NiceZyme view |
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KEGG | KEGG entry |
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MetaCyc | metabolic pathway |
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PRIAM | profile |
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PDB structures | RCSB PDB PDBe PDBsum |
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Search |
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PMC | articles |
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PubMed | articles |
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NCBI | proteins |
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Peptidyl-glycinamidase (EC 3.4.19.2, carboxyamidase, peptidyl carboxy-amidase, peptidyl-aminoacylamidase, carboxamidopeptidase, peptidyl amino acid amide hydrolase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of C-terminal glycinamide from polypeptides
This enzyme inactivates vasopressin and oxytocin by splitting off glycinamide.
References
- ^ Fruhaufová, L.; Suska-Brezezinska, E.; Barth, T.; Rychlik, I. (1973). "Rat liver enzyme inactivating oxytocin and its deamino-carba analogues". Collection of Czechoslovak Chemical Communications. 38 (9): 2793–2798. doi:10.1135/cccc19732793.
- ^ Nardacci NJ, Mukhopadhyay S, Campbell BJ (January 1975). "Partial purification and characterization of the antidiuretic hormone-inactivating enzyme from renal plasma membranes". Biochimica et Biophysica Acta (BBA) - Enzymology. 377 (1): 146–57. doi:10.1016/0005-2744(75)90295-8. PMID 1122284.
- ^ Simmons WH, Walter R (January 1980). "Carboxamidopeptidase: purification and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin". Biochemistry. 19 (1): 39–48. doi:10.1021/bi00542a007. PMID 6766314.
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