EC Number   |
General Information |
Reference |
|---|
    3.5.1.116 | metabolism |
(S)-ureidoglycine aminohydrolase plays a key role in the ureide pathway of purine catabolism of plants and some bacteria |
734179 |
| 3.5.1.116 | metabolism |
the enzyme is involved in the plant ureide pathway, overview |
734481 |
| 3.5.1.116 | more |
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 |
734481 |
| 3.5.1.116 | more |
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 |
734179 |
