Dihidrolipoilizinski-ostatak sukciniltransferaza

Dihidrolipoilizinski-ostatak sukciniltransferaza
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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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 ⇌ {\displaystyle \rightleftharpoons } 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

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  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. 
  • 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. 

Spoljašnje veze

  • MeSH Dihydrolipoyllysine-residue+succinyltransferase
  • 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