Overview:

D-Lactate dehydrogenase catalyzes the conversion of pyruvate into D-lactate, via the oxidation of NADH to NAD+. It can also catalyze the reverse reaction, conversion of D-lactate into pyruvate through the reduction of NAD+ to NADH (1). This reaction is a principal step in the production of d-lactate in lactic acid bacteria (2). Because D-LDH is elevated in a variety of disorders, analysis of total enzyme activity and predominantly its isoenzyme pattern can significantly contribute to the diagnosis of diseases which are linked to tissue damage (3). Applications of this enzyme include enzymatic determination of metabolites such as ATP, ADP, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g., GPT, PK, and CPK.

References:

1. Farhana A, et al. Biochemistry, Lactate Dehydrogenase. [Updated 2022 May 8]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2022 Jan-. Available from: https://www.ncbi.nlm.nih.gov/books/NBK557536/

2. Baolei Jia, et al. Catalytic, Computational, and Evolutionary Analysis of the d-Lactate Dehydrogenases Responsible for d-Lactic Acid Production in Lactic Acid Bacteria. Journal of Agricultural and Food Chemistry 2018 66 (31), 8371-8381 DOI: 10.1021/acs.jafc.8b02454

3. Klein R, et al. Clinical and Diagnostic Significance of Lactate Dehydrogenase and Its Isoenzymes in Animals. Vet Med Int. 2020 Jun 15;2020:5346483. PMID: 32607139