Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NAD+ | exogenous NAD+ stimulates enzyme activity, because a small fraction of hUXS releases the NADH and UDP-alpha-D-4-dehydroxylose intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD+, explaining the apparent stimulatory effect of added cofactor | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, PDB entry 1Z7E | Escherichia coli |
purified recombinant UXS85-420 lacking the N-terminal membrane-spanning domain, hanging drop vapor diffusion method, precipitant containing 1.3 M ammonium sulfate, 0.1 M magnesium formate, and 0.15% PEG at 26°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of decarboxylation reaction, overview | Escherichia coli | |
additional information | - |
additional information | steady-state kinetics of decarboxylation reaction, overview | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | UGA decarboxylase produces NADH and UDP-alpha-D-4-dehyroxylose as products, it can rebind NADH and UDP-alpha-D-4-dehyroxylose to slowly make UDP-alpha-D-xylose | ? | - |
? | |
UDP-alpha-D-glucuronate + NAD+ | Escherichia coli | - |
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
r | |
UDP-alpha-D-glucuronate + NAD+ | Homo sapiens | - |
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | UGA decarboxylase produces NADH and UDP-alpha-D-4-dehyroxylose as products, it can rebind NADH and UDP-alpha-D-4-dehyroxylose to slowly make UDP-alpha-D-xylose | Escherichia coli | ? | - |
? | |
additional information | hUXS contains a bound NAD+ cofactor that it recycles by first oxidizing UDP-alpha-D-glucuronic acid, and then reducing the UDP-alpha-D-4-dehydroxylose to produce UDP-alpha-D-xylose | Homo sapiens | ? | - |
? | |
UDP-alpha-D-glucuronate + NAD+ | - |
Escherichia coli | UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
r | |
UDP-alpha-D-glucuronate + NAD+ | - |
Homo sapiens | UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
ArnA | - |
Escherichia coli |
UDP-alpha-D-xylose synthase | - |
Homo sapiens |
UGA decarboxylase | - |
Escherichia coli |
UXS | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
8 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | induced-fit conformational change associated with cofactor binding, overview | Escherichia coli | |
NAD+ | - |
Escherichia coli | |
NAD+ | NAD+ is buried in the enzyme core catalytic domain, binding structure, overview | Homo sapiens | |
NADH | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the short-chain dehydrogenase/reductase family of nucleotide-sugar modifying enzymes | Homo sapiens |
additional information | induced-fit conformational change associated with cofactor binding, overview | Escherichia coli |