Protein Variants | Comment | Organism |
---|---|---|
C305A | the guaBDELTACBS phenotype can be complemented in trans by a mutant guaB allele, which encodes the catalytically disabled IMPDHC305A protein containing an intact Bateman domain | Escherichia coli |
additional information | deletion of the Bateman domain has no effect on the in vitro IMPDH activity. In vivo deletion of the Bateman domain of IMPDH (guaBDELTACBS) sensitizes the bacterium to growth arrest by adenosine and inosine, thus derepresses the synthesis of AMP from inosine 5'-phosphate. The growth inhibitory effect of inosine can be rescued by second-site suppressor mutations in the genes responsible for the conversion of inosine to AMP (gsk, purA, and purB) as well as by the prsA1 allele, which encodes a 5-phosphoribosyl 1-pyrophosphate synthetase that is insensitive to allosteric inhibition by adenylate nucleotides. The guaBDELTACBS phenotype can be complemented in trans by a mutant guaB allele, which encodes the catalytically disabled IMPDH C305A protein containing an intact Bateman domain | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
inosine 5'-phosphate + NAD+ + H2O | - |
Escherichia coli | xanthosine 5'-phosphate + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IMPDH | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | the Bateman domain of IMPDH is a negative trans-regulator of adenylate nucleotide synthesis, whereby this role is independent of the catalytic function of IMPDH in the de novo GMP biosynthesis | Escherichia coli |