Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for drug development in treatment of structural schizophrenia | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
R418A | site-directed mutagenesis, chemical rescue of the mutant by guanidine, methylguanidine, ethylguanidine, acteamide, and aminoguanidine, not by hydroxyurea, overview | Tritrichomonas suis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
beta-methylene thiazole 4-carboxamide adenine dinucleotide | i.e. beta-Me-TAD or CH2-TAD | Homo sapiens | |
beta-methylene thiazole 4-carboxamide adenine dinucleotide | i.e. beta-Me-TAD | Tritrichomonas suis | |
mizoribine 5'-phosphate | complexes the enzyme | Tritrichomonas suis | |
additional information | the enzyme is resistant to mizoribine 5'-phosphate due to its open dehydrogenase conformation in opposite to the bacterial enzyme which has a closed hydrolase conformation | Homo sapiens | |
Mycophenolic acid | traps the reaction intermediate E-XMP, the human enzyme is sensitive to the inhibitor due to its open dehydrogenase conformation | Homo sapiens | |
ribavirin 5'-phosphate | - |
Homo sapiens | |
ribavirin 5'-phosphate | - |
Tritrichomonas suis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
inosine 5'-phosphate + NAD+ + H2O | Homo sapiens | - |
xanthosine 5'-phosphate + NADH | - |
r | |
inosine 5'-phosphate + NAD+ + H2O | Tritrichomonas suis | - |
xanthosine 5'-phosphate + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Tritrichomonas suis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
IMP + NAD+ + H2O = XMP + NADH + H+ | reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base | Homo sapiens | |
IMP + NAD+ + H2O = XMP + NADH + H+ | reaction and kinetic mechanism, an Arg residue is involved in catalysis as general base, Cys319-linked covalent enzyme intermediate E-XMP | Tritrichomonas suis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
the bacterial enzyme shows low activity due to its open dehydrogenase conformation in opposite to the bacterial enzyme which has a closed hydrolase conformation | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
inosine 5'-phosphate + NAD+ + H2O | - |
Homo sapiens | xanthosine 5'-phosphate + NADH | - |
r | |
inosine 5'-phosphate + NAD+ + H2O | - |
Tritrichomonas suis | xanthosine 5'-phosphate + NADH | - |
r |
Subunits | Comment | Organism |
---|---|---|
tetramer | the enzyme forms a homotetramer with four active sites | Tritrichomonas suis |
tetramer | the enzyme forms a homotetramer with four active sites and an open dehydrogenase conformation | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
IMPDH | - |
Homo sapiens |
IMPDH | - |
Tritrichomonas suis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Homo sapiens | |
NAD+ | - |
Tritrichomonas suis | |
NADH | - |
Homo sapiens | |
NADH | - |
Tritrichomonas suis |