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	additional information	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	additional information	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	additional information	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