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Peptidilna dipeptidaza B
Identifikatori
EC broj	3.4.15.4
CAS broj	147014-93-5
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Peptidilna dipeptidaza B (EC 3.4.15.4, dipeptidilna karboksihidrolaza, atriopeptinska konvertaza, atrijalna di-(tri)peptidilna karboksihidrolaza, peptidilnadipeptidaza B, atrijalna dipeptidilna karboksihidrolaza, atrijalna peptidna konvertaza) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Odvajanje C-terminalnog dipeptida ili u retkim slučajevima tripeptida

Ova membranska, cinkova metalopeptidaza je prisutan u sisarskim atrijalnim miocitima.

Reference

↑ Harris, R.B. and Wilson, I.B. (1984). „Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization”. Arch. Biochem. Biophys. 233: 667-675. PMID 6385859.
↑ Harris, R.B. and Wilson, I.B. (1985). „Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase”. Peptides (Fayetteville) 6: 393-396. PMID 2999723.
↑ Soler, D.F. and Harris, R.B. (1988). „Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position”. Int. J. Peptide Protein Res. 32: 35-40. PMID 3146555.
↑ Soler, D.F. and Harris, R.B. (1989). „Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity”. Peptides (Fayetteville) 10: 63-68. PMID 2501770.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). 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 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Peptidyl-dipeptidase+B

[1] Harris, R.B. and Wilson, I.B. (1984). „Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization”. Arch. Biochem. Biophys. 233: 667-675. PMID 6385859.

[2] Harris, R.B. and Wilson, I.B. (1985). „Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase”. Peptides (Fayetteville) 6: 393-396. PMID 2999723.

[3] Soler, D.F. and Harris, R.B. (1988). „Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position”. Int. J. Peptide Protein Res. 32: 35-40. PMID 3146555.

[4] Soler, D.F. and Harris, R.B. (1989). „Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity”. Peptides (Fayetteville) 10: 63-68. PMID 2501770.

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