Lactate Dehydrogenase
Lactate Dehydrogenase (LDHD) is the mitochondrial D-lactate dehydrogenase, a stereoselective flavoprotein dehydrogenase that acts on D-2-hydroxyacids. It acts specifically on D-lactate rather than L-lactate and prevents the toxic accumulation of D-lactate in the organism. Browse Assay Genie's current range of Lactate Dehydrogenase research reagents below, or read on for the biology behind the target.
Lactate Dehydrogenase (LDHD, lactate dehydrogenase D) is a stereoselective dehydrogenase that targets a wide variety of D-2-hydroxyacids, particularly those with small to moderately sized hydrophobic groups attached to the C2 atom. Its substrates include D-lactate, which is generated in small amounts either endogenously through the methylglyoxal metabolism pathway or exogenously through intestinal bacterial activity and dietary intake. The enzyme acts specifically on D-lactate and not on its stereoisomer L-lactate, and in doing so it prevents the toxic accumulation of D-lactate in the organism.
The enzyme also converts branched-chain D-2-hydroxyacids into branched-chain ketoacids, so it may indirectly regulate branched-chain amino acid metabolism. The protein is localised to the mitochondrion. It belongs to the FAD-binding oxidoreductase/transferase type 4 family, and HGNC places the LDHD gene in the flavoprotein group and the D-lactate dehydrogenase family. The enzyme is assigned EC 1.1.98.-.
According to the NCBI Gene summary, the encoded protein belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. The similar protein in yeast has both D-lactate and D-glycerate dehydrogenase activities. Alternative splicing occurs at this locus, and two transcript variants encoding distinct isoforms have been identified. The mouse ortholog is Ldhd. Researchers studying this LDHD protein should take care to distinguish it from the L-lactate dehydrogenases, which act on the other stereoisomer.
LDHD acts specifically on D-lactate and prevents its toxic accumulation in the organism, making it central to studies of D-lactate handling.
D-lactate is generated endogenously through the methylglyoxal metabolism pathway, which links this enzyme to the fate of that pathway's product.
By converting branched-chain D-2-hydroxyacids into branched-chain ketoacids, LDHD may indirectly regulate branched-chain amino acid metabolism.
As a mitochondrial FAD-binding flavoprotein with stereoselective activity towards D-2-hydroxyacids, LDHD is a useful subject for enzyme specificity studies.
LDHD is a mitochondrial, stereoselective dehydrogenase acting on D-2-hydroxyacids. It acts specifically on D-lactate, not L-lactate, and prevents toxic D-lactate accumulation. It also converts branched-chain D-2-hydroxyacids into ketoacids, so it may indirectly regulate branched-chain amino acid metabolism.
NCBI Gene reports alternative splicing at this locus, with two transcript variants encoding distinct isoforms. The protein belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family and, per UniProt, to the FAD-binding oxidoreductase/transferase type 4 family. Its official name is lactate dehydrogenase D.
The mouse has an ortholog, Ldhd. NCBI Gene also notes that the similar yeast protein has both D-lactate and D-glycerate dehydrogenase activities, indicating a conserved enzyme family. Check the datasheet of any product for its validated reactivity.
Other lactate dehydrogenases and enzymes of lactate and methylglyoxal metabolism with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q86WU2; product specifications from Assay Genie datasheets.