L-Leucine Dehydrogenase, Bacillus cereus

Toxicity: Standard Handling (A)

Native L-leucine dehydrogenase from Bacillus cereus. Purified enzyme that catalyzes the NAD-dependent conversion of L-leucine to α-ketoisocaproate. Suitable for the production of L-tertiary leucine amino acids. Has an optimal pH of 10.5-10.8 for L-leucine substrate and 9.4 for α-ketoisocaproate substrate. Has an optimal temperature of 65°C.

pH optimum 10.5-10.8 (L-leucine substrate) and 9.4 (α-ketoisocaproate substrate), temperature optimum 65°C.

Kärst, U., et al. 1986. FEMS Microbiol. Lett. 37, 335.
Schütte, H., et al. 1985. Appl. Microbiol.Biotechnol.22, 306.

One unit is defined as the amount of enzyme that will convert 1.0 µmol L-leucine to α-ketoisocaproate in the presence of NAD⁺ per min at 30°C, pH 10.7.

In 100 mM NaCl, 10 mM potassium phosphate buffer, 50% glycerol, pH 7.5.

Following initial thaw, aliquot and freeze (-20°C).

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