Dihidrolipoil dehidrogenaza

Dihidrolipoil dehidrogenaza
Dihidrolipoil dehidrogenaza dimer, Pseudomonas putida
Identifikatori
EC broj 1.8.1.4
CAS broj 9001-18-7
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

Dihidrolipoil dehidrogenaza (EC 1.8.1.4, LDP-Glc, LDP-Val, dehidrolipoatna dehidrogenaza, dijaforaza, dihidrolipoamidna dehidrogenaza, dihidrolipoamid:NAD+ oksidoreduktaza, dihidrolipoinska dehidrogenaza, dihidrotioktinska dehidrogenaza, lipoamidna dehidrogenaza (NADH), lipoamidna oksidoreduktaza (NADH), lipoamidna reduktaza, lipoamidna reduktaza (NADH), lipoatna dehidrogenaza, lipoinsko kiselinska dehidrogenaza, lipoilna dehidrogenaza, protein-6-N-(dihidrolipoil)lizin:NAD+ oksidoreduktaza) je enzim sa sistematskim imenom protein-N6-(dihidrolipoil)lizin:NAD+ oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

protein N6-(dihidrolipoil)lizin + NAD+ {\displaystyle \rightleftharpoons } protein N6-(lipoil)lizin + NADH + H+

Ovaj enzim je flavoprotein (FAD). On je komponenta multienzimskog kompleksa 2-okso-kiselinske dehidrogenaze.

Reference

  1. Massey, V. (1963). „Lipoyl dehydrogenase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 275-306. 
  2. Massey, V., Gibson, Q.H. and Veeger, C. (1960). „Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)”. Biochem. J. 77: 341-351. PMID 13767908. 
  3. Savage, N. (1957). „Preparation and properties of highly purified diaphorase”. Biochem. J. 67: 146-155. PMID 13471525. 
  4. Straub, F.B. (1939). „Isolation and properties of a flavoprotein from heart muscle tissue”. Biochem. J. 33: 787-792. PMID 16746974. 
  5. 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. 
  6. Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. (2005). „Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase”. Protein Expr. Purif. 39: 269-282. PMID 15642479. 

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. 

Spoljašnje veze

  • MeSH Dihydrolipoyl+dehydrogenase
  • 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