4-Hidroksi-2-oksoglutaratna aldolaza

4-Hidroksi-2-oksoglutaratna aldolaza
Identifikatori
EC broj 4.1.3.16
CAS broj 9030-81-3
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

4-Hidroksi-2-oksoglutaratna aldolaza (EC 4.1.3.16, 2-okso-4-hidroksiglutaratna aldolaza, hidroksiketoglutarinska aldolaza, 4-hidroksi-2-ketoglutarinska aldolaza, 2-keto-4-hidroksiglutarinska aldolaza, 4-hidroksi-2-ketoglutaratna aldolaza, 2-keto-4-hidroksiglutaratna aldolaza, 2-okso-4-hidroksiglutarinska aldolaza, DL-4-hidroksi-2-ketoglutaratna aldolaza, hidroksiketoglutaratna aldolaza, 2-keto-4-hidroksibutiratna aldolaza, 4-hidroksi-2-oksoglutaratna glioksilat-lijaza, KHGA) je enzim sa sistematskim imenom 4-hidroksi-2-oksoglutarat glioksilat-lijaza (formira piruvat).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

4-hidroksi-2-oksoglutarat {\displaystyle \rightleftharpoons } piruvat + glioksilat

Ovaj enzim deluje na oba enantiomera.

Reference

  1. Kuratomi, K. and Fukunaga, K. (1963). „The metabolism of γ-hydroxyglutamate in rat liver. I. Enzymic synthesis of γ-hydroxy-α-ketoglutarate from pyruvate and glyoxalate”. Biochim. Biophys. Acta 78: 617-628. PMID 14089442. 
  2. Nishihara, H. (1971). „2-Keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserine”. Biochemistry 10: 1353-1364. PMID 5580656. 
  3. Nishihara, H. and Dekker, E.E. (1972). „Purification, substrate specificity and binding, β-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase”. J. Biol. Chem. 247: 5079-5087. PMID 4560498. 
  4. Wood, W.A. (1972). „2-Keto-3-deoxy-6-phosphogluconic and related aldolases”. u: Boyer, P.D.. The Enzymes. 7 (3rd izd.). New York: Academic Press. str. 281-302. 

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. 
  • Wood, W.A. (1972). „2-Keto-3-deoxy-6-phosphogluconic and related aldolases”. u: Boyer, P.D.. The Enzymes. 7 (3rd izd.). New York: Academic Press. str. 281-302. 

Spoljašnje veze

  • MeSH 4-hydroxy-2-oxoglutarate+aldolase
  • 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