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Literature summary for 3.5.3.4 extracted from

  • Shin, I.; Han, K.; Rhee, S.
    Structural insights into the substrate specificity of (S)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase (2014), J. Mol. Biol., 426, 3028-3040.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with allantoate, sitting drop vapor diffusion method, using 0.1 M sodium citrate (pH 5.6), 20% (w/v) polyethylene glycol 4000, 20%(v/v) isopropanol, 1 mMMnCl2, and 5 mM allantoate Escherichia coli

Protein Variants

Protein Variants Comment Organism
E126A inactive Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required for maximum activity Escherichia coli
Mn2+ required for maximum activity Escherichia coli
Ni2+ required for maximum activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
allantoate + H2O Escherichia coli
-
(S)-ureidoglycolate + urea
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77425
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
allantoate + H2O
-
Escherichia coli (S)-ureidoglycolate + urea
-
?

Synonyms

Synonyms Comment Organism
AAH
-
Escherichia coli
allantoate amidohydrolase
-
Escherichia coli