For research use only. Not for therapeutic Use.
L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity[1].
Reaction conditions
Molecular weight:38 kDa (SDS-PAGE)
Isoelectric point:6.2
Optimum pH:6.5
Optimum temperature:45 ℃
pH Stability:4.5-10.0 (37℃,1h)
Thermal stability:<50 ℃ (pH7.4,15min)
Inhibitors:Co2+,Cu2+,Fe3+,Ni2+,Zn2+,NEM,SDS,Proclin
Protocol
The enzyme dissolved in water
Catalog Number | I042549 |
CAS Number | 9001-60-9 |
Purity | ≥95% |
Reference | [1]. Simon ES, et al. D-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids. Appl Biochem Biotechnol. 1989 Nov;22(2):169-79. [2]. Holmberg N, et al. Redesign of the coenzyme specificity in L-lactate dehydrogenase from bacillus stearothermophilus using site-directed mutagenesis and media engineering. Protein Eng. 1999 Oct;12(10):851-6. |