Crystallization (Comment) | Organism |
---|---|
ternary complex of allantoate amidohydrolase with substrate allantoate and a sulfate ion, X-ray diffraction structure determination and analysis at 2.25 A resolution, modelling | Escherichia coli K-12 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
sulfate | an allosteric effector responsible for stabilizing substrate binding | Escherichia coli K-12 | |
Zn2+ | two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases, binding structure, the two zinc ions have subtly different coordination geometries, overview | Escherichia coli K-12 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
allantoate + 2 H2O | Escherichia coli K-12 | one of the crucial alternate steps in purine metabolism, allantoin catabolic pathway, overview | (S)-ureidoglycolate + 2 NH3 + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli K-12 | P77425 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
allantoate + H2O = (S)-ureidoglycine + NH3 + CO2 | catalytic mechanism, substrate specificity, and structure-function relationship, functional role of hinge regions during catalysis for open and closed conformations, overview | Escherichia coli K-12 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
allantoate + 2 H2O | one of the crucial alternate steps in purine metabolism, allantoin catabolic pathway, overview | Escherichia coli K-12 | (S)-ureidoglycolate + 2 NH3 + CO2 | - |
? | |
allantoate + 2 H2O | the enzyme is specific for allantoate, binding involves residues His228, Asn277, Arg290, and His384 | Escherichia coli K-12 | (S)-ureidoglycolate + 2 NH3 + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer, catalytic domain structure, three-dimensional structure analysis revealing an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family. The enzyme lacks the (beta/alpha)8-barrel fold characteristic of the amidohydrolases, overview | Escherichia coli K-12 |
Synonyms | Comment | Organism |
---|---|---|
allantoate amidohydrolase | - |
Escherichia coli K-12 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
above | Escherichia coli K-12 |