Dihidrolipoilizin-ostatak acetiltransferaza

Dihidrolipoilizin-ostatak acetiltransferaza
Identifikatori
EC broj 2.3.1.12
CAS broj 9032-29-5
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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PMC articles
PubMed articles
NCBI Protein search

Dihidrolipoilizin-ostatak acetiltransferaza (EC 2.3.1.12, acetil-KoA:dihidrolipoamidna S-acetiltransferaza, dihidrolipoamidna S-acetiltransferaza, dihidrolipoatna acetiltransferaza, dihidrolipoinska transacetilaza, dihidrolipoilna acetiltransferaza, lipoatna acetiltransferaza, lipoatna transacetilaza, lipoinska acetiltransferaza, lipoinska kiselina acetiltransferaza, lipoinska transacetilaza, lipoilacetiltransferaza, tioltransacetilaza A, transacetilaza X, enzim-dihidrolipoillizin:acetil-KoA S-acetiltransferaza, acetil-KoA:enzim 6-N-(dihidrolipoil)lizin S-acetiltransferaza) je enzim sa sistematskim imenom acetil-KoA:enzim N6-(dihidrolipoil)lizin S-acetiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

acetil-KoA + enzim N6-(dihidrolipoil)lizin {\displaystyle \rightleftharpoons } KoA + enzim N6-(S-acetildihidrolipoil)lizin

Multimer (24-mer ili 60-mer, u zavisnosti od izvora) ovog enzima formira osnovu piruvat dehidrogenaznog multienzimskog kompleksa.

Reference

  1. Brady, R.O. and Stadtman, E.R. (1954). „Enzymatic thioltransacetylation”. J. Biol. Chem. 211: 621-629. PMID 13221570. 
  2. Gunsalus, I.C. (1954). „Group transfer and acyl-generating functions of lipoic acid derivatives”. u: McElroy, W.D. and Glass, B.. A Symposium on the Mechanism of Enzyme Action. Baltimore: Johns Hopkins Press. str. 545-580. 
  3. Gunsalus, I.C., Barton, L.S. and Gruber, W. (1956). „Biosynthesis and structure of lipoic acid derivatives”. J. Am. Chem. Soc. 78: 1763-1766. 
  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. 

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. 
  • Gunsalus, I.C. (1954). „Group transfer and acyl-generating functions of lipoic acid derivatives”. u: McElroy, W.D. and Glass, B.. A Symposium on the Mechanism of Enzyme Action. Baltimore: Johns Hopkins Press. str. 545-580. 

Spoljašnje veze

  • MeSH Dihydrolipoyllysine-residue+acetyltransferase
  • p
  • r
  • u
TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6