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Literature summary for 5.1.1.1 extracted from

  • Morollo, A.A.; Petsko, G.A.; Ringe, D.
    Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase (1999), Biochemistry, 38, 3293-3301.
    View publication on PubMed
Search for more literature for 5.1.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, the structure of the enzyme with the inhibitor propionate bound in the active site is determined by X-ray crystallography to a resolution of 1.9 A Geobacillus stearothermophilus

Inhibitors

Inhibitors Comment Organism Structure
acetate
-
 Geobacillus stearothermophilus
propionate
-
 Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P10724
-
-

Subunits

Subunits Comment Organism
dimer
-
 Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate both active sites of the dimer contain a pyridoxal 5'-phosphate molecule in aldimine linkage to Lys39 as a protonated Schiff base. The protonated pyridoxal 5'-phosphate-Lys39 Schiff base is the reactive form of the enzyme Geobacillus stearothermophilus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
20
-
 propionate
-
 Geobacillus stearothermophilus
92
-
 acetate
-
 Geobacillus stearothermophilus