EC Number   |
General Information |
Reference |
|---|
    1.1.1.27 | evolution |
genes ldh, ldhB and ldhX, are transcribed to some extent in Lactococcus lactis strain MG1363. The product of the ldhX gene has little nLDH activity as well as ldhB which exhibits only leaky transcription and plays a minor role in lactate yield. LDHA encoded by ldh has been found to perform major L-nLDH activity, with the contribution of other alternate L-nLDHs being small |
-, 740458 |
| 1.1.1.27 | evolution |
sequence identity between the Enterococcus mundtii LDH-1 and LDH-2 is 44.9% |
-, 740460 |
| 1.1.1.27 | evolution |
there are two types of L-nLDHs, non-allosteric L-nLDHs and allosteric L-nLDHs |
-, 741368 |
| 1.1.1.27 | malfunction |
LDH-5 inhibitors decrease mitochondrial membrane potential and elevate intracellular oxidative stress that diminishes the ability of cells to proliferate, reduces their metastatic potential, and increases sensitivity to chemotherapeutic drugs. Inhibitors can also act as a blocker of the LDH-5ssDNA interactions to prevent RNA synthesis. miR-34a is a direct repressor of LDHA gene expression. Inhibiting LDHA expression may reduce the invasive and metastatic potential of cancer cells by decreasing their proliferation ability and reversing their resistance to chemotherapy. Enzyme inhibitors NHI-1 and -2 used together with gemcitabine enhance the antiproliferative and anti-invasive activities of the chemotherapeutic drug, under both normoxia and hypoxia, in pancreatic ductal adenocarcinoma (PDAC) cell lines. Inhibitor NIH-2, combined with the redox-dependent bioreductive anticancer prodrug EO9, synergistically induces p53-positive cancer cell death |
740255 |
| 1.1.1.27 | malfunction |
loss of water-forming NADH oxidase NOX activity in Streptococcus mutans leads to Rex-mediated overcompensation in NAD+ regeneration by lactate dehydrogenase. The altered transcriptome and metabolome of the DELTAnox strain are sufficient to impair its ability to compete with commensal peroxigenic oral streptococci during growth under aerobic conditions, phenotype, overview |
-, 740628 |
| 1.1.1.27 | malfunction |
silencing LDHB selectively inhibits the proliferation of both oxidative and glycolytic cancer cells over normal cells, targeting LDHB selectively blocks autophagy in oxidative and glycolytic cancer cells, but siLDHB does not affect the subcellular distribution pattern of lysosomes and their distance to the cell nucleus. siLDHB induces lysosomal inhibition in oxidative cancer cells. Overexpression of LDHB decreases the number of acidic vesicles per cell. LDHB overexpression increases mature autolysosome formation and intracellular proteolysis in SiHa and in HeLa cells. LDHB reaction substrate lactate and product pyruvate do not metabolically restore autophagy and intracellular proteolysis in LDHB-depleted SiHa cells, but LDHB-depleted cells switch to a glycolytic metabolism |
740254 |
| 1.1.1.27 | metabolism |
L-lactate dehydrogenase (LDHA) is a substrate of protein tyrosine phosphatase PTP1B. LDHA enrichment ias significantly lower in PTP1B knockdown cell lysate compared to untreated and scrambled siRNA controls |
760891 |
| 1.1.1.27 | metabolism |
L-lactate dehydrogenase is an important enzyme involved in the last step of glycolysis that catalyzes the reversible conversion of pyruvate to L-lactate with the simultaneous oxidation of NADH to NAD+ |
721235 |
| 1.1.1.27 | metabolism |
lactate dehydrogenase (LDH) is a glycolytic enzyme that catalyzes the final step of glycolysis and produces NAD+ |
740001 |
| 1.1.1.27 | metabolism |
lactate dehydrogenase-5 (LDH-5) is a central player in theWarburg effect which catalyzes the formation of lactate in the final step of the glycolytic pathway |
740255 |
