Glycyl endopeptidase
Glycyl endopeptidase | |||||||||
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Identifiers | |||||||||
EC number | 3.4.22.25 | ||||||||
CAS number | 149719-24-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya proteinase 4, PPIV, chymopapain M) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Preferential cleavage: Gly-, in proteins and small molecule substrates
This enzyme is isolated from the papaya plant, Carica papaya.
References
- ↑ Polgár, L. (1981). "Isolation of highly active papaya peptidases A and B from commercial chymopapain". Biochim. Biophys. Acta. 658: 262–269. doi:10.1016/0005-2744(81)90296-5. PMID 7018581.
- ↑ Buttle, D.J.; Kembhavi, A.A.; Sharp, S.L.; Shute, R.E.; Rich, D.H.; Barrett, A.J. (1989). "Affinity purification of the novel cysteine proteinase papaya proteinase IV and papain from papaya latex". Biochem. J. 261: 469–476. PMID 2505761.
- ↑ Ritonja, A.; Buttle, D.J.; Rawlings, N.D.; Turk, V.; Barrett, A.J. (1989). "Papaya proteinase IV amino acid sequence". FEBS Lett. 258: 109–112. doi:10.1016/0014-5793(89)81627-8. PMID 2591528.
- ↑ Buttle, D.J.; Ritonja, A.; Pearl, L.H.; Turk, V.; Barrett, A.J. (1990). "Selective cleavage of glycyl bonds by papaya proteinase IV". FEBS Lett. 260: 195–197. doi:10.1016/0014-5793(90)80101-n. PMID 2404797.
- ↑ Buttle, D.J.; Ritonja, A.; Dando, P.M.; Abrahamson, M.; Shaw, E.N.; Wikstrom, P.; Turk, V.; Barrett, A.J. (1990). "Interaction of papaya proteinase IV with inhibitors". FEBS Lett. 262: 58–60. doi:10.1016/0014-5793(90)80153-a. PMID 1690669.
External links
- Glycyl endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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