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Alfa-litička endopeptidaza
Identifikatori
EC broj	3.4.21.12
CAS broj	37288-76-9
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

Alfa-litička endopeptidaza (EC 3.4.21.12, miksobakter alfa-litička proteinaza, alfa-litička proteinaza, alfa-litička proteaza, Mycobakterija sorangium alfa-litička proteinaza, Myxobacter 495 alfa-litička proteinaza, Myxobacter alfa-litička proteinaza) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Preferentno odvajanje: Ala-, Val- u bakterijskim ćelijskim zidovima, elastinu i drugim proteinima

Ovaj enzim je izolovan iz miksobakterije Lysobacter enzimogena.

Reference

↑ Olson, M.O.J., Nagabushan, N., Dzwiniel, M., Smillie, L.B. and Whitaker, D.R. (1970). „Primary structure of α-lytic protease: a bacterial homologue of the pancreatic serine proteases”. Nature 228: 438-442. PMID 5482494.
↑ Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.
↑ Epstein, D.M. and Wensink, P.C. (1988). „The α-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes”. J. Biol. Chem. 263: 16586-16590. PMID 3053694.
↑ Bone, R., Frank, D., Kettner, C.A. and Agard, D.A. (1989). „Structural analysis of specificity: α-lytic protease complexes with analogues of reaction intermediates”. Biochemistry 28: 7600-7609. PMID 2611204.

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.

Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.

Vanjske veze

MeSH Alpha-lytic+endopeptidase

[1] Olson, M.O.J., Nagabushan, N., Dzwiniel, M., Smillie, L.B. and Whitaker, D.R. (1970). „Primary structure of α-lytic protease: a bacterial homologue of the pancreatic serine proteases”. Nature 228: 438-442. PMID 5482494.

[2] Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.

[3] Epstein, D.M. and Wensink, P.C. (1988). „The α-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes”. J. Biol. Chem. 263: 16586-16590. PMID 3053694.

[4] Bone, R., Frank, D., Kettner, C.A. and Agard, D.A. (1989). „Structural analysis of specificity: α-lytic protease complexes with analogues of reaction intermediates”. Biochemistry 28: 7600-7609. PMID 2611204.

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