PROSITE documentation PDOC00332Alanine racemase pyridoxal-phosphate attachment site
Alanine racemase (EC 5.1.1.1) [1] catalyzes the pyridoxal-dependent conversion of L-alanine into D-alanine, a key building block of bacterial peptidoglycan. In bacteria such as Escherichia coli or Salmonella typhimurium, there are two forms of alanine racemase: a biosynthetic form (alr) required for cell wall formation and a form (dadB) that functions in L-alanine catabolism. In contrast to dadB and alr which are monomeric enzymes, the alanine racemase of Bacillaceae are homodimers.
The pyridoxal-phosphate group of alanine racemase is attached to a lysine residue. The sequence around this residue is highly conserved in all forms of the enzyme.
Last update:February 2002 / Pattern revised.
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| 1 | Authors | Hayashi H. Wada H. Yoshimura T. Esaki N. Soda K. |
| Title | Recent topics in pyridoxal 5'-phosphate enzyme studies. | |
| Source | Annu. Rev. Biochem. 59:87-110(1990). | |
| PubMed ID | 2197992 | |
| DOI | 10.1146/annurev.bi.59.070190.000511 |
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