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Link to original content: http://en.wikipedia.org/wiki/Beta-peptidyl_aminopeptidase
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Beta-peptidyl aminopeptidase

From Wikipedia, the free encyclopedia
Beta-peptidyl aminopeptidase
Identifiers
EC no.3.4.11.25
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

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  1. ^ Heck T, Limbach M, Geueke B, Zacharias M, Gardiner J, Kohler HP, Seebach D (December 2006). "Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides". Chemistry & Biodiversity. 3 (12): 1325–48. doi:10.1002/cbdv.200690136. PMID 17193247. S2CID 38292191.
  2. ^ Geueke B, Namoto K, Seebach D, Kohler HP (September 2005). "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. doi:10.1128/jb.187.17.5910-5917.2005. PMC 1196161. PMID 16109932.
  3. ^ Geueke B, Heck T, Limbach M, Nesatyy V, Seebach D, Kohler HP (December 2006). "Bacterial beta-peptidyl aminopeptidases with unique substrate specificities for beta-oligopeptides and mixed beta,alpha-oligopeptides". The FEBS Journal. 273 (23): 5261–72. doi:10.1111/j.1742-4658.2006.05519.x. PMID 17064315. S2CID 84167461.
  4. ^ Heck T, Kohler HP, Limbach M, Flögel O, Seebach D, Geueke B (September 2007). "Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes". Chemistry & Biodiversity. 4 (9): 2016–30. doi:10.1002/cbdv.200790168. PMID 17886858. S2CID 85123861.
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