L-galactose 1-dehydrogenase

L-galactose 1-dehydrogenase (EC 1.1.1.316, L-GalDH, L-galactose dehydrogenase) is an enzyme with the 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+
L-galactose 1-dehydrogenase
Identifiers
EC number1.1.1.316
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 (September 2004). "Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate". Plant & Cell Physiology. 45 (9): 1271–9. doi:10.1093/pcp/pch152. PMID 15509850.
  2. Gatzek S, Wheeler GL, Smirnoff N (June 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". The Plant Journal. 30 (5): 541–53. doi:10.1046/j.1365-313x.2002.01315.x. PMID 12047629.
  3. Wheeler GL, Jones MA, Smirnoff N (May 1998). "The biosynthetic pathway of vitamin C in higher plants". Nature. 393 (6683): 365–9. doi:10.1038/30728. PMID 9620799.
  4. Oh MM, Carey EE, Rajashekar CB (July 2009). "Environmental stresses induce health-promoting phytochemicals in lettuce". Plant Physiology and Biochemistry. 47 (7): 578–83. doi:10.1016/j.plaphy.2009.02.008. PMID 19297184.
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