{PDOC00332}
{PS00395; ALANINE_RACEMASE}
{BEGIN}
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* Alanine racemase pyridoxal-phosphate attachment site *
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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.

-Consensus pattern: [SACVLG]-[AIPTV]-x(0,1)-K-[ADGS]-[DEN]-[GA]-Y-G-[HACILN]-
                    [GD]
                    [K is the pyridoxal-P attachment site]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2002 / Pattern revised.

[ 1] Hayashi H., Wada H., Yoshimura T., Esaki N., Soda K.
     "Recent topics in pyridoxal 5'-phosphate enzyme studies."
     Annu. Rev. Biochem. 59:87-110(1990).
     PubMed=2197992; DOI=10.1146/annurev.bi.59.070190.000511
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