EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
- |
Escherichia coli |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
- |
Methylomonas aminofaciens |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
- |
Escherichia coli K-12 |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
stereochemistry |
Escherichia coli K-12 |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
substrate binding structure |
Escherichia coli |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
SgaH/UlaD and SgbH |
Escherichia coli K-12 |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | 3-dehydro-L-gulonate 6-phosphate + H+ |
step in the catabolic pathway of L-ascorbate utilization |
Escherichia coli K-12 |
L-xylulose 5-phosphate + CO2 |
- |
? |
| 4.1.1.85 | more |
enzyme catalyzes one step in the L-ascorbate utilization pathway, L-ascorbate is converted to L-xylulose, overview |
Escherichia coli K-12 |
? |
- |
? |
| 4.1.1.85 | more |
enzymes SgaH/UlaD and SgbH are not active with 3-dehydro-L-gulonate |
Escherichia coli K-12 |
? |
- |
? |
| 4.1.1.85 | more |
the D-arabino-hex-3-ulose 6-phosphate synthase of Methylomonas aminofaciens also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction with lower activity than for the preferred reaction catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, proton exchange reaction rates, overview |
Methylomonas aminofaciens |
? |
- |
? |
