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Kandidapepsin
Identifikatori
EC broj	3.4.23.24
CAS broj	69458-91-9
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

Kandidapepsin (EC 3.4.23.24, Candida albicans aspartinska proteinaza, Candida albicans karboksilna proteinaza, Candida albicans sekretorna kiselinska proteinaza, Candida olea kiselinska proteinaza, Candida aspartinska proteinaza, Candida olea aspartinska proteinaza, Candida albicans aspartinsk proteinaza) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Preferentno razlaganje na karboksilnim ili hidrofobnim aminokiselinama. Ne dolazi do razlaganja Leu¹⁵-Tyr, Tyr16-Leu i Phe^{24^{-Phe lanaca insulina B. Dolazi do aktivacije tripsinogena, i degradacije keratina}}

Ova endopeptidaza je prisutna u gljivi Candida albicans.

Reference

↑ Remold, H., Fasold, H. and Staib, F. (1968). „Purification and characterization of a proteolytic enzyme from Candida albicans”. Biochim. Biophys. Acta 167: 399-406. PMID 5729955.
↑ Rüchel, R. (1981). „Properties of a purified proteinase from the yeast Candida albicans”. Biochim. Biophys. Acta 659: 99-113. PMID 7018586.
↑ Negi, M., Tsuboi, R., Matsui, T. and Ogawa, H. (1984). „Isolation and characterization of proteinase from Candida albicans: substrate specificity”. J. Invest. Dermatol. 83: 32-36. PMID 6203988.
↑ Lott, T.J., Page, L.S., Boiron, P., Benson, J. and Reiss, E. (1989). „Nucleotide sequence of the Candida albicans aspartyl proteinase gene”. Nucleic Acids Res. 17: 1779-1779. PMID 2646602.

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 Candidapepsin

[1] Remold, H., Fasold, H. and Staib, F. (1968). „Purification and characterization of a proteolytic enzyme from Candida albicans”. Biochim. Biophys. Acta 167: 399-406. PMID 5729955.

[2] Rüchel, R. (1981). „Properties of a purified proteinase from the yeast Candida albicans”. Biochim. Biophys. Acta 659: 99-113. PMID 7018586.

[3] Negi, M., Tsuboi, R., Matsui, T. and Ogawa, H. (1984). „Isolation and characterization of proteinase from Candida albicans: substrate specificity”. J. Invest. Dermatol. 83: 32-36. PMID 6203988.

[4] Lott, T.J., Page, L.S., Boiron, P., Benson, J. and Reiss, E. (1989). „Nucleotide sequence of the Candida albicans aspartyl proteinase gene”. Nucleic Acids Res. 17: 1779-1779. PMID 2646602.

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