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Literature summary extracted from

  • Agarwal, R.; Burley, S.K.; Swaminathan, S.
    Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics (2007), J. Mol. Biol., 368, 450-463.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.3.9 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

EC Number Metals/Ions Comment Organism Structure
3.5.3.9 sulfate an allosteric effector responsible for stabilizing substrate binding Escherichia coli K-12
3.5.3.9 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.9 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

EC Number Organism UniProt Comment Textmining
3.5.3.9 Escherichia coli K-12 P77425
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.3.9 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.9 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
-
 ?
3.5.3.9 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

EC Number Subunits Comment Organism
3.5.3.9 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

EC Number Synonyms Comment Organism
3.5.3.9 allantoate amidohydrolase
-
 Escherichia coli K-12

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.3.9 8
-
 above Escherichia coli K-12