EC Number   |
General Information |
Reference |
|---|
    1.1.1.215 | malfunction |
gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism |
-, 761153 |
| 1.1.1.215 | metabolism |
in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD. The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE (EC 1.1.1.366). The genes coding for these two enzymes are clustered and share the same bidirectional promoter |
-, 761153 |
| 1.1.1.215 | more |
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity |
-, 742168 |
| 1.1.1.215 | physiological function |
a GluD deletion mutant does not show reduced growth when cultivated on agar plate with D-glucuronate as sole carbon source. In the liquid cultivation on D-glucuronate, 2-oxo-L-gulonate accumulates in the medium after D-glucuronate is consumed |
-, 761153 |
| 1.1.1.215 | physiological function |
deletion of the gluC gene results in a phenotype of no growth on D-glucuronate |
741418 |
| 1.1.1.215 | physiological function |
Gluconobacter oxydans NBRC3293 produces 2,5-dioxo-D-gluconate from D-glucose via D-gluconate and 2-keto-D-gluconate, with accumulation of the product in the culture medium, the efficiency of 2,5-diketo-D-gluconate production is unsatisfactory because there is a large amount of residual D-gluconate at the end of the biotransformation process. Heterologous overexpression of the kgdSLC genes in a mutant strain of Gluconobacter japonicus NBRC3271 engineered to produce 2-dehydro-D-gluconate efficiently from a mixture of D-glucose and D-gluconate, results in a mutant strain that consumes almost all of the starting materials (D-glucose and D-gluconate) to produce 2,5-dioxo-D-gluconate quantitatively as a seemingly unique metabolite |
-, 739910 |
| 1.1.1.215 | physiological function |
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction, cf. EC 1.1.1.272 |
-, 742168 |
