Biology:Xanthomonalisin
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| Xanthomonalisin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.101 | ||||||||
| CAS number | 113356-29-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Xanthomonalisin (EC 3.4.21.101, Xanthomonas aspartic proteinase, xanthomonapepsin, sedolisin-B) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Cleavage of casein
This enzyme is secreted by the bacterium Xanthomonas sp.
References
- ↑ Oda, K.; Nakazima, T.; Terashita, T.; Suzuki, K.; Murao, S. (1987). "Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium". Agric. Biol. Chem. 51: 3073-3080. doi:10.1271/bbb1961.51.3073.
- ↑ Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Dunn, B.M.; Oda, K. (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochim. Pol. 50: 81-102. PMID 12673349.
External links
- Xanthomonalisin at the US National Library of Medicine Medical Subject Headings (MeSH)
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