Dihidrolipoilizinski-ostatak sukciniltransferaza
| Dihidrolipoilizinski-ostatak sukciniltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Homo 24-mer katalitička domena | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.3.1.61 | ||||||||
| CAS broj | 9032-28-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Dihidrolipoilizinski-ostatak sukciniltransferaza (EC 2.3.1.61, dihidrolipoamidna S-sukciniltransferaza, dihidrolipoamidna sukciniltransferaza, dihidrolipoinska transsukcinilaza, dihidrolipolil transsukcinilaza, dihidrolipoil transsukcinilaza, lipoat sukciniltransferaza (Escherichia coli), lipoinska transsukcinilaza, lipoilna transsukcinilaza, sukcinil-KoA:dihidrolipoamid S-sukciniltransferaza, sukcinil-KoA:dihidrolipoat S-sukciniltransferaza, enzim-dihidrolipoillizin:sukcinil-KoA S-sukciniltransferaza) je enzim sa sistematskim imenom sukcinil-KoA:enzim-N6-(dihidrolipoil)lizin S-sukciniltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- sukcinil-KoA + enzim N6-(dihidrolipoil)lizin KoA + enzim N6-(S-sukcinildihidrolipoil)lizin
Multimer (24-mer) ovog enzima formira srž multienzimskog kompleksa, i čvrsto vezuje EC 1.2.4.2, oksoglutaratnu dehidrogenaza (sukcinilni transfer) i EC 1.8.1.4, dihidrolipoilnu dehidrogenazu.
Reference[uredi | uredi kod]
- ↑ Derosier, D.J., Oliver, R.M. and Reed, L.J. (1971). „Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex”. Proc. Natl. Acad. Sci. USA 68: 1135-1137. PMID 4942179.
- ↑ Reed, L.J. and Cox, D.J. (1970). „Multienzyme complexes”. u: Boyer, P.D.. The Enzymes. 1 (3rd izd.). New York: Academic Press. str. 213-240.
- ↑ Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. (1998). „Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex”. J. Mol. Biol. 280: 655-668. PMID 9677295.
- ↑ 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[uredi | uredi kod]
- 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.
- Reed, L.J. and Cox, D.J. (1970). „Multienzyme complexes”. u: Boyer, P.D.. The Enzymes. 1 (3rd izd.). New York: Academic Press. str. 213-240.