Cloned (Comment) | Organism |
---|---|
- |
Cryptosporidium parvum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.006 | - |
NAD+ | pH 8.0, 25°C | Homo sapiens | |
0.14 | - |
NAD+ | - |
Cryptosporidium parvum | |
0.19 | - |
acetylpyridine adenine dinucleotide | - |
Cryptosporidium parvum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cryptosporidium parvum | - |
- |
- |
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
to more than 95% purity | Cryptosporidium parvum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O | - |
Homo sapiens | xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide | - |
? | |
inosine 5'-phosphate + acetylpyridine adenine dinucleotide + H2O | - |
Cryptosporidium parvum | xanthosine 5'-phosphate + reduced acetylpyridine adenine dinucleotide | - |
? | |
inosine 5'-phosphate + NAD+ + H2O | IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites | Cryptosporidium parvum | xanthosine 5'-phosphate + NADH + H+ | - |
? | |
inosine 5'-phosphate + NAD+ + H2O | IMPDH catalyzes a dehydrogenase reaction and a hydrolysis reaction, a redox step producing NADH and the covalent intermediate E-xanthosine 5'-monophosphate* and a hydrolysis step that produces xanthosine 5'-monophosphate. The enzyme toggles between the open conformation required for the dehydrogenase reaction and the closed conformation of the hydrolase reaction by moving a mobile flap into the NAD site. The dehydrogenase and hydrolase reactions display significant differences in the host (Homo sapiens) and parasite (Cryptosporidium parvum) enzymes, in keeping with the phylogenetic and structural divergence of their active sites | Homo sapiens | xanthosine 5'-phosphate + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IMPDH | - |
Cryptosporidium parvum |
IMPDH2 | - |
Homo sapiens |
inosine-5'-monophosphate dehydrogenase | - |
Homo sapiens |
inosine-5'-monophosphate dehydrogenase | - |
Cryptosporidium parvum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.39 | - |
NAD+ | pH 8.0, 25°C | Homo sapiens | |
2.6 | - |
NAD+ | - |
Cryptosporidium parvum | |
3 | - |
acetylpyridine adenine dinucleotide | - |
Cryptosporidium parvum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | acetylpyridine adenine dinucleotide | Cryptosporidium parvum | |
NAD+ | - |
Homo sapiens | |
NAD+ | - |
Cryptosporidium parvum |