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Rizopuspepsin
Identifikatori
EC broj	3.4.23.21
CAS broj	2620497
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

Rizopuspepsin (EC 3.4.23.21, Rhizopus aspartinska proteinaza, neuraza, Rhizopus kiselinska proteaza, Rhizopus kiselinska proteinaza) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Hidroliza proteina sa širokom specifičnošću, slično pepsinu A. Postoji preferencija za hidrofobne ostatake u P1 i P1'. Dolazi do zgrušavanja mleka i aktivacije tripsinogena. Ne dolazi do razlaganja Gln⁴-His, ali se razlaže His¹⁰-Leu i Val¹²-Glu u B lancu insulina

Ovaj enzim je prisutan u gljivi Rhizopus chinensis.

Reference

↑ Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and Fukumoto, J. (1969). „Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis”. Agric. Biol. Chem. 33: 1419-1426.
↑ Kurono, Y., Chidimatsu, M., Horikoshi, K. and Ikeda, Y. (1971). „Isolation of a protease from a Rhizopus product”. Agric. Biol. Chem. 35: 1668-1675.
↑ Ohtsuru, M., Tang, J. and Delaney, R. (1982). „Purification and characterization of rhizopuspesin isozymes from a liquid culture of Rhizopus chinensis”. Int. J. Biochem. 14: 925-932. PMID 6751894.
↑ Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. (1987). „Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action”. Proc. Natl. Acad. Sci. USA 84: 7009-7013. PMID 3313384.

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 Rhizopuspepsin

[1] Tsuru, D., Hattori, A., Tsuji, H., Yamamoto, T. and Fukumoto, J. (1969). „Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis”. Agric. Biol. Chem. 33: 1419-1426.

[2] Kurono, Y., Chidimatsu, M., Horikoshi, K. and Ikeda, Y. (1971). „Isolation of a protease from a Rhizopus product”. Agric. Biol. Chem. 35: 1668-1675.

[3] Ohtsuru, M., Tang, J. and Delaney, R. (1982). „Purification and characterization of rhizopuspesin isozymes from a liquid culture of Rhizopus chinensis”. Int. J. Biochem. 14: 925-932. PMID 6751894.

[4] Suguna, K., Padlan, E.A., Smith, C.W., Carlson, W.D. and Davies, D.R. (1987). „Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action”. Proc. Natl. Acad. Sci. USA 84: 7009-7013. PMID 3313384.

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