| L-galactose 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 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+
The enzyme catalyses a step in the ascorbate biosynthesis in higher plants.
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Transcription
References
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links
- L-galactose+1-dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This page was last edited on 26 August 2023, at 14:40