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Peptidil-Lys metaloendopeptidaza
Peptidil-Lys metaloendopeptidaza
Identifikatori
EC broj	3.4.24.20
CAS broj	65979-41-1
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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NCBI	proteini

Peptidil-Lys metaloendopeptidaza (EC 3.4.24.20, Armillaria mellea neutralna proteinaza, peptidilnalizinska metaloproteinaza) je enzim.^[1]^[2] Ovaj enzim katalizuje sledeću hemijsku reakciju

Preferentno razlaganje proteina: -Xaa-Lys (gde Xaa može da bude Pro)

Ovaj enzim je prisutan u gljivi Armillaria mellea.

Reference

^ Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F (1975). „The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues”. Biochem. J. 149: 497—506. PMID 1239277.
^ Lewis, W.G., Basford, J.M. and Walton, P.L. (1978). „Specificity and inhibition studies of Armillaria mellea protease”. Biochim. Biophys. Acta. 522: 551—560. PMID 23849.

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.

Spoljašnje veze

Peptidyl-Lys+metalloendopeptidase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, Bossa F, Barra D, Carloni M, Fasella P, Riva F (1975). „The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues”. Biochem. J. 149: 497—506. PMID 1239277.

[2] Lewis, W.G., Basford, J.M. and Walton, P.L. (1978). „Specificity and inhibition studies of Armillaria mellea protease”. Biochim. Biophys. Acta. 522: 551—560. PMID 23849.

[1]

[2]