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Aspartatna 4-dekarboksilaza
	Aspartatna 4-dekarboksilaza dodekamer, Comamonas testosteroni
Identifikatori
EC broj	4.1.1.12
CAS broj	9024-57-1
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

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. and 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. and 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 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 Aspartate+4-decarboxylase

[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. and 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. and 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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