Beta-peptidyl aminopeptidase
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| 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
- ↑ Heck, T., Limbach, M., Geueke, B., Zacharias, M., Gardiner, J., Kohler, H.P. and Seebach, D. (2006). "Enzymatic degradation of β- and mixed α,β-oligopeptides". Chem. Biodivers. 3: 1325–1348. PMID 17193247.
- ↑ Geueke, B., Namoto, K., Seebach, D. and Kohler, H.P. (2005). "A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri- and β-dipeptides". J. Bacteriol. 187: 5910–5917. PMID 16109932.
- ↑ Geueke, B., Heck, T., Limbach, M., Nesatyy, V., Seebach, D. and Kohler, H.P. (2006). "Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides". FEBS J. 273: 5261–5272. PMID 17064315.
- ↑ Heck, T., Kohler, H.P., Limbach, M., Flögel, O., Seebach, D. and Geueke, B. (2007). "Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes". Chem. Biodivers. 4: 2016–1030. PMID 17886858.
External links
- Beta-peptidyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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