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Literature summary for 5.1.1.1 extracted from

  • Yoshimura, T.; Esaki, N.; Soda, K.
    Structure and function of alanine racemase (1992), Bull. Inst. Chem. Res. Kyoto Univ., 70, 378-384.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
additional information double mutant for the alr encoded enzyme and the dad B encoded enzyme display a phenotype of requirement for exogenous D-Ala for growth Salmonella enterica subsp. enterica serovar Typhimurium
additional information mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Salmonella enterica subsp. enterica serovar Typhimurium alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Enterococcus faecalis
-
-
-
Geobacillus stearothermophilus
-
-
-
Pseudomonas putida
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala
-
Salmonella enterica subsp. enterica serovar Typhimurium D-Ala
-
?
L-Ala
-
Bacillus subtilis D-Ala
-
?
L-Ala
-
Geobacillus stearothermophilus D-Ala
-
?
L-Ala
-
Pseudomonas putida D-Ala
-
?
L-Ala
-
Enterococcus faecalis D-Ala
-
?
additional information alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Geobacillus stearothermophilus
monomer
-
Enterococcus faecalis
monomer dadB enzyme and alr enzyme Salmonella enterica subsp. enterica serovar Typhimurium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
80 min, pH 7.2, stable Salmonella enterica subsp. enterica serovar Typhimurium

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.2
-
80°C, stable Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated Salmonella enterica subsp. enterica serovar Typhimurium
pyridoxal 5'-phosphate pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated Bacillus subtilis
pyridoxal 5'-phosphate pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated Geobacillus stearothermophilus
pyridoxal 5'-phosphate pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated Enterococcus faecalis
pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme Salmonella enterica subsp. enterica serovar Typhimurium
pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme Bacillus subtilis
pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme Geobacillus stearothermophilus
pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme Enterococcus faecalis