EC Number   |
General Information |
Reference |
|---|
   5.1.1.21 | evolution |
the enzyme belongs to the fold-type I subgroup of pyridoxal 5'-phosphate-dependent enzymes and is very close to aminobutyrate aminotransferases family |
-, 747208 |
| 5.1.1.21 | evolution |
the enzyme is a eukaryotic member of a large and widely conserved phenazine biosynthesis protein PhzF-like protein family and belongs to a D-amino acid racemase gene family. The phenazine biosynthesis-like protein family (PF02567), which is closely related to the DAP epimerase (PF01678), proline racemase (PF05544), and PrpF (PF04303) families |
749170 |
| 5.1.1.21 | evolution |
the enzyme is a fold-type I racemase |
746630 |
| 5.1.1.21 | malfunction |
a daar1 enzyme knockout mutant shows highly reduced levels of N-malonyl-D-allo-isoleucine |
749170 |
| 5.1.1.21 | more |
exploitation of natural metabolic variation by integrating metabolomics with genome-wide association as an approach for functional genomics study of specialized metabolism |
749170 |
| 5.1.1.21 | more |
identification of the active site residues responsible for its nonpolar amino acid recognition and reactivity specificity from structure comparisons with the alpha-amino-epsilon-caprolactam racemase (EC 5.1.1.15) from Achromobacter obae and the cystathionine beta-lyase (EC 4.4.1.8) from Escherichia coli (PDB IDs 2ZUK and 3DXW), active site structure, overview |
-, 747208 |
| 5.1.1.21 | more |
the enzyme is a fold-type I racemase, similar to the alpha-amino-epsilon-caprolactam racemase (EC 5.1.1.15). The active-site cavity in the apoenzyme structure is much more solvent-accessible than that in the pyridoxal 5'-phosphate-bound structure. A marked structural change occurs around the active site upon binding of pyridoxal 5'-phosphate that provides a solvent-inaccessible environment for the enzymatic reaction. Detailed enzyme structure analysis and structure comparisons, active site and substrate/ligand-binding structre, structure-function relationship, overview |
746630 |
| 5.1.1.21 | physiological function |
the amino acid racemase is responsible for the biosynthesis of N-malonyl-D-allo-isoleucine. DAAR1 does not use a N-derivatized substrate and the malonylation of D-amino acids occurs downstream in the metabolic pathway |
749170 |
