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PubMed	članci
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Aspartatna 4-dekarboksilaza
Aspartatna 4-dekarboksilaza
	Aspartatna 4-dekarboksilaza dodekamer, Comamonas testosteroni
Identifikatori
EC broj	4.1.1.12
CAS broj	9024-57-1
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
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Aspartatna 4-dekarboksilaza (EC 4.1.1.12, desulfinaza, aminomalonska dekarboksilaza, aspartatna beta-dekarboksilaza, aspartatna omega-dekarboksilaza, aspartinska omega-dekarboksilaza, aspartinska beta-dekarboksilaza, L-aspartatna beta-dekarboksilaza, cistein sulfinska desulfinaza, L-cistein sulfinatno kiselinska desulfinaza, L-aspartatna 4-karboksi-lijaza) je enzim sa sistematskim imenom L-aspartat 4-karboksi-lijaza (formira L-alanin).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-aspartat

\rightleftharpoons

L-alanin + CO₂

Ovaj enzim je piridoksal-fosfatni protein.

Reference

^ Kakimoto, T., Kato, J., Shibitani, T., Nishimura, N. and Chibata, I. (1969). „Crystalline L-aspartate β-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties”. J. Biol. Chem. 244: 353—358. PMID 5773301.
^ Novogrodsky, A. & Meister, A. (1964). „Control of aspartate β-decarboxylase activity by transamination”. J. Biol. Chem. 239: 879—888. PMID 14154469.
^ Palekar, A.G., Tate, S.S. and Meister, A. (1970). „Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine”. Biochemistry. 9: 2310—2315. PMID 5424207.
^ Wilson, E.M. & Kornberg, H.L. (1963). „Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp”. Biochem. J. 88: 578—587. PMID 14071532.

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

Aspartate+4-decarboxylase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Kakimoto, T., Kato, J., Shibitani, T., Nishimura, N. and Chibata, I. (1969). „Crystalline L-aspartate β-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties”. J. Biol. Chem. 244: 353—358. PMID 5773301.

[2] Novogrodsky, A. & Meister, A. (1964). „Control of aspartate β-decarboxylase activity by transamination”. J. Biol. Chem. 239: 879—888. PMID 14154469.

[3] Palekar, A.G., Tate, S.S. and Meister, A. (1970). „Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine”. Biochemistry. 9: 2310—2315. PMID 5424207.

[4] Wilson, E.M. & Kornberg, H.L. (1963). „Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp”. Biochem. J. 88: 578—587. PMID 14071532.

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