L-galactose 1-dehydrogenase

L-galactose 1-dehydrogenase
Identifiers
EC number 1.1.1.316
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

L-galactose 1-dehydrogenase (EC 1.1.1.316, L-GalDH, L-galactose dehydrogenase) is an enzyme with systematic name L-galactose:NAD+ 1-oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction

L-galactose + NAD+ L-galactono-1,4-lactone + NADH + H+

The enzyme catalyses a step in the ascorbate biosynthesis in higher plants.

References

  1. Mieda, T.; Yabuta, Y.; Rapolu, M.; Motoki, T.; Takeda, T.; Yoshimura, K.; Ishikawa, T.; Shigeoka, S. (2004). "Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate". Plant Cell Physiol. 45 (9): 1271–1279. doi:10.1093/pcp/pch152. PMID 15509850.
  2. Gatzek, S.; Wheeler, G.L.; Smirnoff, N. (2002). "Antisense suppression of L-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated L-galactose synthesis". Plant J. 30 (5): 541–553. doi:10.1046/j.1365-313x.2002.01315.x. PMID 12047629.
  3. Wheeler, G.L.; Jones, M.A.; Smirnoff, N. (1998). "The biosynthetic pathway of vitamin C in higher plants". Nature. 393: 365–369. doi:10.1038/30728. PMID 9620799.
  4. Oh, M.M.; Carey, E.E.; Rajashekar, C.B. (2009). "Environmental stresses induce health-promoting phytochemicals in lettuce". Plant Physiol. Biochem. 47 (7): 578–583. doi:10.1016/j.plaphy.2009.02.008. PMID 19297184.
This article is issued from Wikipedia - version of the 5/21/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.