Beta-peptidyl aminopeptidase

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

  1. 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. doi:10.1002/cbdv.200690136. PMID 17193247.
  2. 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. doi:10.1128/jb.187.17.5910-5917.2005. PMID 16109932.
  3. 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. doi:10.1111/j.1742-4658.2006.05519.x. PMID 17064315.
  4. 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. doi:10.1002/cbdv.200790168. PMID 17886858.

External links

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