PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30931947-2 2019 We illustrate this with the identification of two different homozygous variants resulting in enzymatic loss-of-function in LDHD, encoding lactate dehydrogenase D, in two unrelated patients with elevated D-lactate urinary excretion and plasma concentrations. Lactic Acid 203-212 lactate dehydrogenase D Homo sapiens 123-127 30931947-2 2019 We illustrate this with the identification of two different homozygous variants resulting in enzymatic loss-of-function in LDHD, encoding lactate dehydrogenase D, in two unrelated patients with elevated D-lactate urinary excretion and plasma concentrations. Lactic Acid 203-212 lactate dehydrogenase D Homo sapiens 138-161 30931947-4 2019 D-lactate levels are rescued by wildtype LDHD but not by patients" variant LDHD, confirming these variants" loss-of-function effect. Lactic Acid 0-9 lactate dehydrogenase D Homo sapiens 41-45 30931947-5 2019 This work provides the first in vivo evidence that LDHD is responsible for human D-lactate metabolism. Lactic Acid 81-90 lactate dehydrogenase D Homo sapiens 51-55 27237045-0 2016 Carbon Flux Trapping: Highly Efficient Production of Polymer-Grade d-Lactic Acid with a Thermophilic d-Lactate Dehydrogenase. Lactic Acid 67-80 lactate dehydrogenase D Homo sapiens 101-124 26265307-0 2015 Development of an enzymatic assay system of D-lactate using D-lactate dehydrogenase and a UV-LED fluorescent spectrometer. Lactic Acid 44-53 lactate dehydrogenase D Homo sapiens 60-83 26265307-2 2015 D-Lactate dehydrogenase (D-LDH) was utilized to catalyze D-lactate and NAD(+) to pyruvate and NADH, respectively. Lactic Acid 57-66 lactate dehydrogenase D Homo sapiens 0-23 26265307-2 2015 D-Lactate dehydrogenase (D-LDH) was utilized to catalyze D-lactate and NAD(+) to pyruvate and NADH, respectively. Lactic Acid 57-66 lactate dehydrogenase D Homo sapiens 25-30 16348833-2 1992 The method is based on an enzymatic stereospecific reaction involving d-(-)-lactate dehydrogenase and linked to a staining reaction; the diffusion area of the d-(-)- isomer stains red around the d-(-)- and the dl-lactic acid-producing colonies, while the colonies producing exclusively l-(+)-lactic acid are detected by the absence of the colored halo. Lactic Acid 213-224 lactate dehydrogenase D Homo sapiens 70-97 23333299-0 2013 Prostate cancer cells metabolize d-lactate inside mitochondria via a D-lactate dehydrogenase which is more active and highly expressed than in normal cells. Lactic Acid 33-42 lactate dehydrogenase D Homo sapiens 69-92 22344644-0 2012 Relative catalytic efficiency of ldhL- and ldhD-encoded products is crucial for optical purity of lactic acid produced by lactobacillus strains. Lactic Acid 98-109 lactate dehydrogenase D Homo sapiens 43-47 22344644-2 2012 Our findings suggest that the relative catalytic efficiencies of ldhL- and ldhD-encoded products are crucial for the optical purity of lactic acid produced by Lactobacillus strains. Lactic Acid 135-146 lactate dehydrogenase D Homo sapiens 75-79 18968259-1 2001 An amperometric biosensor was constructed for the analysis of d-lactic acid based on immobilizing d-lactate dehydrogenase(d-LDH), alanine aminotransferase (ALT), NAD(+), a redox polymer and polyethylenimine in carbon paste. Lactic Acid 62-75 lactate dehydrogenase D Homo sapiens 98-121 15987839-4 2005 More recent studies reported that mammals have a relatively high capacity for D-lactate metabolism and identified a putative mammalian D-lactate dehydrogenase. Lactic Acid 78-87 lactate dehydrogenase D Homo sapiens 135-158 16348833-2 1992 The method is based on an enzymatic stereospecific reaction involving d-(-)-lactate dehydrogenase and linked to a staining reaction; the diffusion area of the d-(-)- isomer stains red around the d-(-)- and the dl-lactic acid-producing colonies, while the colonies producing exclusively l-(+)-lactic acid are detected by the absence of the colored halo. Lactic Acid 287-303 lactate dehydrogenase D Homo sapiens 70-97 7074087-1 1982 Initial rate measurements were made of the oxidation of D-lactate and D-alpha-hydroxybutyrate by oxygen and potassium ferricyanide, catalyzed by D-lactate dehydrogenase from Megasphera elsdenii. Lactic Acid 56-65 lactate dehydrogenase D Homo sapiens 145-168 1456422-1 1992 A fluorimetric assay for D-lactate in human blood samples was developed using an endpoint enzymatic assay with D-lactate dehydrogenase from Staphylococcus epidermidis. Lactic Acid 25-34 lactate dehydrogenase D Homo sapiens 111-134 34258137-1 2021 Background: d-lactate, one of the isomers of lactate, exists in a low concentration in healthy individuals and it can be oxidized to pyruvate catalyzed by d-lactate dehydrogenase. Lactic Acid 45-52 lactate dehydrogenase D Homo sapiens 155-178 35080666-10 2022 Overall, the proportion of lactate in the general catabolic carbon flow increased from 2.9% (wild type) to 28.5% in the LDH-overproducing mutant. Lactic Acid 27-34 lactate dehydrogenase D Homo sapiens 120-123 3243781-1 1988 D-Lactate in biological samples was converted into the hydrazone of pyruvate in the presence of D-lactate dehydrogenase, an NADH-reoxidation system using diaphorase, DL-6,8-thioctamide and hydrazine. Lactic Acid 0-9 lactate dehydrogenase D Homo sapiens 96-119 3690825-1 1987 We describe a method for the direct assay of D(-)lactate in plasma using D(-)lactate dehydrogenase and a color reagent to produce a formazan color measured at 510 nm. Lactic Acid 45-56 lactate dehydrogenase D Homo sapiens 73-98 6698613-4 1984 Alternatively, treatment with base released D-lactate (beta-elimination), which was identified fluorimetrically by reduction of NAD to NADH with D-lactate dehydrogenase. Lactic Acid 44-53 lactate dehydrogenase D Homo sapiens 145-168 7074088-1 1982 The reaction of oxidized D-lactate dehydrogenase with D-lactate and reduced D-lactate dehydrogenase with pyruvate and oxygen was studied in a stopped-flow spectrophotometer. Lactic Acid 25-34 lactate dehydrogenase D Homo sapiens 76-99 31638601-3 2019 We demonstrate that gout can be caused by a mutation in LDHD within the putative catalytic site of the encoded d-lactate dehydrogenase, resulting in augmented blood levels of d-lactate, a stereoisomer of l-lactate, which is normally present in human blood in miniscule amounts. Lactic Acid 111-120 lactate dehydrogenase D Homo sapiens 56-60 259500-5 1978 A stereospecific assay was used to measure D-lactate in human plasma; it involved the spectrophotometric analysis of NADH at 340 nm catalysed by D-lactate dehydrogenase (D-lactate:NAD+ oxidoreductase; EC 1.1.1.28) from Lactobacillus leichmannii. Lactic Acid 43-52 lactate dehydrogenase D Homo sapiens 145-168 31638601-3 2019 We demonstrate that gout can be caused by a mutation in LDHD within the putative catalytic site of the encoded d-lactate dehydrogenase, resulting in augmented blood levels of d-lactate, a stereoisomer of l-lactate, which is normally present in human blood in miniscule amounts. Lactic Acid 204-213 lactate dehydrogenase D Homo sapiens 56-60 31638601-3 2019 We demonstrate that gout can be caused by a mutation in LDHD within the putative catalytic site of the encoded d-lactate dehydrogenase, resulting in augmented blood levels of d-lactate, a stereoisomer of l-lactate, which is normally present in human blood in miniscule amounts. Lactic Acid 204-213 lactate dehydrogenase D Homo sapiens 111-134