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3-Aminobutiril-KoA amonijak-lijaza
3-Aminobutiril-KoA amonijak-lijaza
Identifikatori
EC broj	4.3.1.14
CAS broj	55467-41-9
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
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NCBI	proteini

3-Aminobutiril-KoA amonijak-lijaza (EC 4.3.1.14, L-3-aminobutiril-KoA deaminaza, L-3-aminobutiril-KoA amonijak-lijaza) je enzim sa sistematskim imenom L-3-aminobutiril-KoA amonijak-lijaza (formira krotonoil-KoA).^[1]^[2] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-3-aminobutiril-KoA

\rightleftharpoons

krotonoil-KoA + NH₃

Hidroksilamin može da zameni amonijak kao supstrat.

Reference

^ Jeng, I.-M., Barker, H.A. (1974). „Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium”. J. Biol. Chem. 249: 6578—6584. PMID 4420467.
^ Barker, H.A., Kahn, J.M., Chew, S. (1980). „Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp”. J. Bacteriol. 143: 1165—1170. PMID 7410315.

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

3-aminobutyryl-CoA+ammonia-lyase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Jeng, I.-M., Barker, H.A. (1974). „Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium”. J. Biol. Chem. 249: 6578—6584. PMID 4420467.

[2] Barker, H.A., Kahn, J.M., Chew, S. (1980). „Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp”. J. Bacteriol. 143: 1165—1170. PMID 7410315.

[1]

[2]