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Oksoglutarat dehidrogenaza (sukcinil-transfer)
Identifikatori
EC broj	1.2.4.2
CAS broj	2604577
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

Oksoglutarat dehidrogenaza (sukcinil-transfer) (EC 1.2.4.2, 2-ketoglutaratna dehidrogenaza, 2-oksoglutaratna dehidrogenaza, 2-oksoglutarat:lipoat oksidoreduktaza, 2-oksoglutarat:lipoamid 2-oksidoreduktaza (dekarboksilacija i akceptor-sukcinilacija), alfa-ketoglutaratna dehidrogenaza, dehidrogenaza alfaketoglutarinska kiselina, alfa-ketoglutarinska dehidrogenaza, alfa-oksoglutaratna dehidrogenaza, AKGDH, OGDC, ketoglutarinska dehidrogenaza, oksoglutaratna dekarboksilaza, oksoglutaratna dehidrogenaza, oksoglutaratna dehidrogenaza (lipoamid)) je enzim sa sistematskim imenom 2-oksoglutarat:(dihidrolipoillizin-ostatak sukciniltransferaza)-lipoillizin 2-oksidoreduktaza (dekarboksilacija, akceptor-sukcinilacija).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

2-oksoglutarat + [dihidrolipoillizin-ostatak sukciniltransferaza] lipoillizin

\rightleftharpoons

[dihidrolipoillizin-ostatak sukciniltransferaza] S-sukcinildihidrolipoillizin + CO₂

Ovaj enzim sadrži tiaminski difosfat. On je komponenta multienzimskog kompleksa 2-oksoglutaratna dehidrogenaza u kome su višestruke kopije vezane za osnovu molekula EC 2.3.1.61, dihidrolipoillizinski-ostatak sukciniltransferaza, koji takođe vezuje višestruke kopije enzima EC 1.8.1.4, dihidrolipoil dehidrogenaze. Ovaj enzim ne deluje na slobodni lipoamid ili lipoillizin, nego samo na lipoilizinski ostatak u EC 2.3.1.61.

Reference

↑ Massey, V. (1960). „The composition of the ketoglutarate dehydrogenase complex”. Biochim. Biophys. Acta 38: 447-460. PMID 14422131.
↑ Ochoa, S. (1954). „Enzymic mechanisms in the citric acid cycle”. Adv. Enzymol. Relat. Subj. Biochem. 15: 183-270. PMID 13158180.
↑ Sanadi, D.R., Littlefield, J.W. and Bock, R.M. (1952). „Studies on α-ketoglutaric oxidase. II. Purification and properties”. J. Biol. Chem. 197: 851-862. PMID 12981117.
↑ Perham, R.N. (2000). „Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions”. Annu. Rev. Biochem. 69: 961-1004. PMID 10966480.

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 Oxoglutarate+dehydrogenase+(succinyl-transferring)

[1] Massey, V. (1960). „The composition of the ketoglutarate dehydrogenase complex”. Biochim. Biophys. Acta 38: 447-460. PMID 14422131.

[2] Ochoa, S. (1954). „Enzymic mechanisms in the citric acid cycle”. Adv. Enzymol. Relat. Subj. Biochem. 15: 183-270. PMID 13158180.

[3] Sanadi, D.R., Littlefield, J.W. and Bock, R.M. (1952). „Studies on α-ketoglutaric oxidase. II. Purification and properties”. J. Biol. Chem. 197: 851-862. PMID 12981117.

[4] Perham, R.N. (2000). „Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions”. Annu. Rev. Biochem. 69: 961-1004. PMID 10966480.

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