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+ \rightleftharpoons 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. and 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. and 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. and 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. and 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.

External links

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