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Keyword
- X-ray crystallography2
- 2-keto-L-gulonic acid1
- aldo-keto reductase1
- ascorbic acid1
- benzylisoquinoline alkaloids1
- biosynthesis1
- D-isomer-specific 2-hydroxyacid dehydrogenase1
- docking1
- enzyme kinetics1
- enzyme structure1
- grapevine1
- morphine1
- N-methyltransferase1
- plant biochemistry1
- protein crystallization1
- secondary metabolism1
- stereoselectivity1
- structural biology1
- structure-function relationship1
- tartaric acid synthesis1
- Vitis vinifera1
Plant Biology
2 Results
- Plant BiologyOpen Access
An aldo-keto reductase with 2-keto-l-gulonate reductase activity functions in l-tartaric acid biosynthesis from vitamin C in Vitis vinifera
Journal of Biological ChemistryVol. 294Issue 44p15932–15946Published online: September 4, 2019- Yong Jia
- Crista A. Burbidge
- Crystal Sweetman
- Emi Schutz
- Kathy Soole
- Colin Jenkins
- and others
Cited in Scopus: 12Tartaric acid has high economic value as an antioxidant and flavorant in food and wine industries. l-Tartaric acid biosynthesis in wine grape (Vitis vinifera) uses ascorbic acid (vitamin C) as precursor, representing an unusual metabolic fate for ascorbic acid degradation. Reduction of the ascorbate breakdown product 2-keto-l-gulonic acid to l-idonic acid constitutes a critical step in this l-tartaric acid biosynthetic pathway. However, the underlying enzymatic mechanisms remain obscure. Here, we identified a V. - ArticleOpen Access
Structure–function studies of tetrahydroprotoberberine N-methyltransferase reveal the molecular basis of stereoselective substrate recognition
Journal of Biological ChemistryVol. 294Issue 40p14482–14498Published online: August 7, 2019- Dean E. Lang
- Jeremy S. Morris
- Michael Rowley
- Miguel A. Torres
- Vook A. Maksimovich
- Peter J. Facchini
- and others
Cited in Scopus: 10Benzylisoquinoline alkaloids (BIAs) are a structurally diverse class of plant-specialized metabolites that have been particularly well-studied in the order Ranunculales. The N-methyltransferases (NMTs) in BIA biosynthesis can be divided into three groups according to substrate specificity and amino acid sequence. Here, we report the first crystal structures of enzyme complexes from the tetrahydroprotoberberine NMT (TNMT) subclass, specifically for GfTNMT from the yellow horned poppy (Glaucium flavum).