EC Number   |
General Information |
Reference |
|---|
    5.1.1.1 | evolution |
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes |
-, 726630, 727440 |
| 5.1.1.1 | evolution |
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme |
748310 |
| 5.1.1.1 | evolution |
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes |
-, 748310 |
| 5.1.1.1 | evolution |
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. The genome sequences of methanogenic archaeon, Methanococcus maripaludis reveals the presence of alanine dehydrogenase gene adjacent to genes for alanine racemase and alanine permease, apparently acquired from bacteria |
748310 |
| 5.1.1.1 | evolution |
alanine racemase is a fold type III pyridoxal-5'-phosphate-dependent amino acid racemase enzyme |
748310 |
| 5.1.1.1 | evolution |
in bacteria, two types of alanine racemase are encoded independently by two genes named dadX and alr. The dadX gene encodes a catabolic alanine racemase DadX, which catalyzes direct conversion of L-Ala to D-Ala. Its expression is induced by L- or D-Ala. The alr gene encodes an anabolic alanine racemase Alr, it is expressed constitutively at low level and essential for providing abundant D-Ala for peptidoglycan biosynthesis. Some bacteria only contain one type alanine racemase gene, whereas others have two of them. Thermoanaerobacter tengcongensis strain MB4 contains two annotated alanine racemase genes MBalr1 and MBalr2. Both genes encode 388 amino acids long alanine racemase, sharing a 58.3% amino acid sequence identity. Compared with MBAlr2, MBAlr1 shows very low catalytic efficiency and limited substrate spectrum. It is probable that MBAlr1 serves as an anabolic and MBAlr2 as the catabolic alanine racemase in Thermoanaerobacter tengcongensis strain MB4 |
749061 |
| 5.1.1.1 | evolution |
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining |
-, 759787 |
| 5.1.1.1 | evolution |
the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes |
-, 746985 |
| 5.1.1.1 | evolution |
the enzyme shows evolutionary and structural similarity to the promiscuous enzymes serine hydroxymethyltransferase, EC 2.1.2.1, and threonine aldolase, EC 4.1.2.48. The three enzymes represent a model of divergent evolution from an ancestral enzyme that was able to catalyse all the reactions of the modern enzymes. Similarly to serine hydroxymethyltransferase and threonine aldolase, Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions |
726814 |
| 5.1.1.1 | evolution |
two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala |
-, 749368 |
