3.5.1.116: ureidoglycolate amidohydrolase
This is an abbreviated version!
For detailed information about ureidoglycolate amidohydrolase, go to the full flat file.
Word Map on EC 3.5.1.116
-
3.5.1.116
-
allantoin
-
allantoate
-
purine
-
ureide
-
ammonia
-
glyoxylate
-
allantoicase
-
legumes
-
aminohydrolase
-
allophanate
- 3.5.1.116
- allantoin
- allantoate
- purine
-
ureide
- ammonia
- glyoxylate
- allantoicase
-
legumes
-
aminohydrolase
- allophanate
Reaction
Synonyms
(S)-ureidoglycine aminohydrolase, (S)-ureidoglycolate amidohydrolase, allA, amidase, ureidoglycolate, AtUAH, EC 3.5.3.19, OsUAH, UAH, UGDA, UGLYAH, ureidoglycolate amidohydrolase, ureidoglycolate hydrolase
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 3.5.1.116 - ureidoglycolate amidohydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Mn2+
Mn2+ is required for maximum catalytic activity. The bimetal reaction center of the enzyme is located at the pocket enclosed by the catalytic domain, dimerization domain, and other structural elements from a different subunit, structure, overview
Mn2+
substrate (S)-ureidoglycine is bound to the Mn2+ ion at the active site of homooctameric enzyme. The Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction