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Beta-peptidilna aminopeptidaza
Beta-peptidilna aminopeptidaza
Identifikatori
EC broj	3.4.11.25
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
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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

^ 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., FlÃ¶gel, 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

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.

Spoljašnje veze

Beta-peptidyl+aminopeptidase на US National Library of Medicine Medical Subject Headings (MeSH)

[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., FlÃ¶gel, 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.

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