Galaktonolakton dehidrogenaza

Galaktonolakton dehidrogenaza
Identifikatori
EC broj 1.3.2.3
CAS broj 2603847
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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Galaktonolakton dehidrogenaza (EC 1.3.2.3, L-galaktono-gama-laktonska dehidrogenaza, L-galaktono-gama-lakton:fericitohrom-c oksidoreduktaza, GLDHaza, GLDazae) je enzim sa sistematskim imenom L-galaktono-1,4-lakton:fericitohrom-c oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) L-galakto-1,4-lakton + 2 fericitohrom c ⇌ {\displaystyle \rightleftharpoons } L-askorbat + 2 ferocitohrom c + 2 H+;;
(2) L-askorbat + 2 fericitohrom c ⇌ {\displaystyle \rightleftharpoons } L-dehidroaskorbat + 2 ferocitohrom c + 2 H+ (spontaneous)

Ovaj enzim katalizuje finalni korak biosinteze L-askorbnske kiseline kod viših biljki i kod skoro svih viših životinja izuzev primata i nekih ptica. Enzim je veoma specifičana za svoj supstrat L-galaktono-1,4-lakton, dok D-galaktono-gama-lakton, D-gulono-gama-lakton, L-gulono-gama-lakton, D-eritronski-gama-lakton, D-ksilonski-gama-lakton, L-manono-gama-lakton, D-galaktonat, D-glukuronat i D-glukonat nisu supstrati.

Reference

  1. ↑ Mapson, L.W. and Breslow, E. (1957). „Properties of partially purified L-galactono-γ-lactone dehydrogenase”. Biochem. J. 65: 29-29. 
  2. ↑ Mapson, L.W., Isherwood, F.A. and Chen, Y.T. (1954). „Biological synthesis of L-ascorbic acid: the conversion of L-galactono-γ-lactone into L-ascorbic acid by plant mitochondria”. Biochem. J. 56: 21-28. PMID 13126087. 
  3. ↑ Isherwood, F.A., Chen, Y.T. and Mapson, L.W. (1954). „Synthesis of L-ascorbic acid in plants and animals.”. Biochem. J. 56: 1-15. PMID 13126085. 
  4. ↑ Ôba, K., Ishikawa, S., Nishikawa, M., Mizuno, H. and Yamamoto, T. (1995). „Purification and properties of L-galactono-γ-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots”. J. Biochem. (Tokyo) 117: 120-124. PMID 7775377. 
  5. ↑ Østergaard, J., Persiau, G., Davey, M.W., Bauw, G. and Van Montagu, M. (1997). „Isolation of a cDNA coding for L-galactono-γ-lactone dehydrogenase, an enzyme involved in the biosynthesis of ascorbic acid in plants. Purification, characterization, cDNA cloning, and expression in yeast”. J. Biol. Chem. 272: 30009-30016. PMID 9374475. 

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 L-galactonolactone+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