Beta-peptidilna aminopeptidaza

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Beta-peptidilna aminopeptidaza
Identifikatori
EC broj 3.4.11.25
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures

Beta-peptidilna aminopeptidaza (EC 3.4.11.25, BapA) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Oslobađanje N-terminalne beta-homoamino kiseline sa peptida koji se sastoje od 2 do 6 aminokiselina

Sphingosinicella xenopeptidilytica vrsta 3-2W4 može da koristi beta-peptide beta-homoVal-beta-homoAla-beta-homoLeu i beta-homoAla-beta-homoLeu kao jedini izvor ugljenika i energije.

Reference[uredi - уреди]

  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. 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. 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. 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. PMID 17886858. 

Literatura[uredi - уреди]

Vanjske veze[uredi - уреди]