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PROSITE documentation PDOC00332

Alanine racemase pyridoxal-phosphate attachment site





Description

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.

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Last update:

February 2002 / Pattern revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ALANINE_RACEMASE, PS00395; Alanine racemase pyridoxal-phosphate attachment site  (PATTERN)


Reference

1AuthorsHayashi H. Wada H. Yoshimura T. Esaki N. Soda K.
TitleRecent topics in pyridoxal 5'-phosphate enzyme studies.
SourceAnnu. Rev. Biochem. 59:87-110(1990).
PubMed ID2197992
DOI10.1146/annurev.bi.59.070190.000511



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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