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Literature summary for 5.1.1.1 extracted from

  • Au, K.; Ren, J.; Walter, T.S.; Harlos, K.; Nettleship, J.E.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.
    Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P) (2008), Acta Crystallogr. Sect. F, F64, 327-333.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
amplified by PCR, cloned and overexpressed with pOPINB in Escherichia coli Rosetta pLysS cells, His-tagged product Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme is subjected to a reductive-methylation procedure Bacillus anthracis

Inhibitors

Inhibitors Comment Organism Structure
(R)-1-aminoethylphosphonic acid in combination with pyridoxal 5'-phosphate Bacillus anthracis

Localization

Localization Comment Organism GeneOntology No. Textmining
exosporium
-
Bacillus anthracis 43592
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43810
-
mass-spectrometry Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine Bacillus anthracis
-
D-alanine enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis r

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81VF6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine
-
Bacillus anthracis D-alanine enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis r

Subunits

Subunits Comment Organism
dimer crystallography Bacillus anthracis

Synonyms

Synonyms Comment Organism
BA0252
-
Bacillus anthracis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate C-terminal region of 1 subdomain: Arg138 donates a hydrogen bond to the phenolic O atom of PLP, Arg224 donates a hydrogen bond to the pyridinyl N atom of PLP, Lys41 forms an aldimine linkage with the PLP, eliminating water to form the Schiff base, C-terminal atoms of second subunit Ser209, Gly226 and Ile227 stabilize the PLP phosphate with the help of Ser209 O(gamma), Tyr45 O(eta) and Tyr359 O(eta) Bacillus anthracis