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Results 1 - 8 of 8
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21evolution the enzyme belongs to the fold-type I subgroup of pyridoxal 5'-phosphate-dependent enzymes and is very close to aminobutyrate aminotransferases family -, 747208
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21evolution the enzyme is a fold-type I racemase 746630
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21malfunction a daar1 enzyme knockout mutant shows highly reduced levels of N-malonyl-D-allo-isoleucine 749170
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21more exploitation of natural metabolic variation by integrating metabolomics with genome-wide association as an approach for functional genomics study of specialized metabolism 749170
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21more 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
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21more 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
Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.21physiological 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
Results 1 - 8 of 8