D-Lactate dehydrogenase, Microorganism  (Synonyms: D-LDH)

D-Lactate dehydrogenase, Microorganism (D-LDH) is an oxidoreductase that uses NAD⁺ or NADP⁺ as an acceptor and acts on the donor CH-OH group, and can catalyze the oxidation of D-lactate to pyruvate. D-Lactate dehydrogenase widely exists in bacteria and fungi, and is often used in biochemical research^[1].

Product Information
Isoelectric point: 4.0
Michaelis constan:1.6×10^-4 M (pyruvate, pH 7.0)
Inhibitors: Ag⁺, Hg²⁺, SH^-reagents
Optimum pH: 6.0-7.0
Optimum temperature: 35-40°C
pH Stability: 5.0-9.0

Instructions
The enzyme can be dissolved in 0.1 M K-phosphate buffer, pH 7.4 or water, or according to the specific experimental reference.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9028-36-8

Solid

White to off-white

[D-Lactate dehydrogenase, Microorganism]

1.1.1.28

≥800 U/mg protein

One unit will convert one micromole of pyruvate to D-lactateper min at pH 7.4 at 25℃.

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. O Dym, et al. The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9413-8.  [Content Brief]