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Literature summary for 5.1.1.1 extracted from

  • Okubo, Y.; Yokoigawa, K.; Esaki, N.; Soda, K.; Misono, H.
    High catalytic activity of alanine racemase from psychrophilic Bacillus psychrosaccharolyticus at high temperatures in the presence of pyridoxal 5'-phosphate (2000), FEMS Microbiol. Lett., 192, 169-173.
    View publication on PubMed

General Stability

General Stability Organism
pyridoxal 5'-phosphate present in the solvent suppresses the enzyme's unfolding Peribacillus psychrosaccharolyticus

Organism

Organism UniProt Comment Textmining
Peribacillus psychrosaccharolyticus
-
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Peribacillus psychrosaccharolyticus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 70 40°C: about 60% of maximal activity, 70°C: about 50% of maximal activity Peribacillus psychrosaccharolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
the decrease in the enzyme activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate, no effect on stability at lower temperatures, 0-30°C Peribacillus psychrosaccharolyticus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km at 30°C is 0.005 mM. Maximal activity is obtained in presence of more than 0.125 mM pyridoxal 5'-phosphate. The decrease in activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate Peribacillus psychrosaccharolyticus