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
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3.5.1.116
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allantoin
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allantoate
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purine
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ureide
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ammonia
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glyoxylate
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allantoicase
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legumes
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aminohydrolase
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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
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General Information
General Information on EC 3.5.1.116 - ureidoglycolate amidohydrolase
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metabolism
additional information
(S)-ureidoglycine aminohydrolase plays a key role in the ureide pathway of purine catabolism of plants and some bacteria
metabolism
the enzyme is involved in the plant ureide pathway, overview
amino acid and structure comparisons, e.g. to allantoate amidinohydrolase, enzyme monomer structure modeling, overview. Monomeric AtUAH (Asn54 to Asp476) is composed of 13 alpha-helices, 12 beta-strands, and 2 short 310-helices. It folds largely into two structural domains: a catalytic domain (residues 54-275 and 392-476) and a dimerization domain (residues 276-391) that is inserted between beta6 and alpha11 of the catalytic domain. The two structural domains are connected by a so-called hinge region (residues 273-275 and 392-394), structure-function analysis, overview. The catalytic domain exhibits an alpha/beta/alpha-folded architecture. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
additional information
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amino acid and structure comparisons, e.g. to allantoate amidinohydrolase, enzyme monomer structure modeling, overview. Monomeric AtUAH (Asn54 to Asp476) is composed of 13 alpha-helices, 12 beta-strands, and 2 short 310-helices. It folds largely into two structural domains: a catalytic domain (residues 54-275 and 392-476) and a dimerization domain (residues 276-391) that is inserted between beta6 and alpha11 of the catalytic domain. The two structural domains are connected by a so-called hinge region (residues 273-275 and 392-394), structure-function analysis, overview. The catalytic domain exhibits an alpha/beta/alpha-folded architecture. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
additional information
the Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. Kinetic analysis characterizes the functional roles of the active site residues, including the Mn2+ ion binding site and residues in the vicinity of (S)-ureidoglycine, structure of the enzyme and its possible catalytic mechanism, overview. The crystal structure of monomeric AtUGlyAH, which contains the ordered residues Pro39 to Leu298, is composed of 19 beta-strands and 4 short 310-helices. Residues Tyr287 and Lys291 are essential for enzyme activity, possibly by dictating the orientation of the ureido and carboxyl groups of the substrate, respectively