Biology:Beta-peptidyl aminopeptidase
From HandWiki
Short description: Class of enzymes
| Beta-peptidyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.25 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Beta-peptidyl aminopeptidase (EC 3.4.11.25, BapA) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction:
- Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids
Sphingosinicella xenopeptidilytica strain 3-2W4 could use beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu as only source of carbon and energy.
References
- ↑ "Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides". Chemistry & Biodiversity 3 (12): 1325–48. December 2006. doi:10.1002/cbdv.200690136. PMID 17193247.
- ↑ "A novel beta-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic beta-tri- and beta-dipeptides". Journal of Bacteriology 187 (17): 5910–7. September 2005. doi:10.1128/jb.187.17.5910-5917.2005. PMID 16109932.
- ↑ "Bacterial beta-peptidyl aminopeptidases with unique substrate specificities for beta-oligopeptides and mixed beta,alpha-oligopeptides". The FEBS Journal 273 (23): 5261–72. December 2006. doi:10.1111/j.1742-4658.2006.05519.x. PMID 17064315.
- ↑ "Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes". Chemistry & Biodiversity 4 (9): 2016–30. September 2007. doi:10.1002/cbdv.200790168. PMID 17886858.
External links
- Beta-peptidyl+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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