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Seikagaku. the Journal of Japanese... Jun 1992
Review
Topics: Amino Acid Sequence; Base Sequence; Female; Humans; Isoenzymes; L-Lactate Dehydrogenase; Male; Molecular Sequence Data
PubMed: 1506717
DOI: No ID Found -
Extremophiles : Life Under Extreme... Nov 20222-Keto-3-deoxy- D-gluconate (KDG) is an important intermediate found in various sugars, sugar acids and polysaccharide catabolic pathways. Here, we report that a...
A functionally uncharacterized type-2 malate/L-lactate dehydrogenase family protein from Thermus thermophilus HB8 catalyzes stereospecific reduction of 2-keto-3-deoxy-D-gluconate.
2-Keto-3-deoxy- D-gluconate (KDG) is an important intermediate found in various sugars, sugar acids and polysaccharide catabolic pathways. Here, we report that a functionally uncharacterized type-2 malate/L-lactate dehydrogenase family protein (TTHB078) from Thermus thermophilus HB8 catalyzes a novel reaction, NAD(P)H-dependent reductase activity on KDG. This enzyme, designated KdgG, utilizes both NADH and NADPH as electron donors, but higher activity was observed with NADH. Analysis of the reaction product revealed that KdgG catalyzes reversible reduction of KDG to form 3-deoxy-D-mannonate. Molecular phylogenetic analysis indicated that KdgG and its homologs distributed in the genus Thermus form a novel clade among type-2 malate/L-lactate dehydrogenase family proteins.
Topics: L-Lactate Dehydrogenase; Thermus thermophilus; Malates; Lactic Acid; NAD; Phylogeny
PubMed: 36416985
DOI: 10.1007/s00792-022-01282-z -
Molecules (Basel, Switzerland) Nov 2021Plasmodium lactate dehydrogenase (pLH) is one of the enzymes in glycolysis with potential target for chemotherapy. This study aimed to clone, overexpress and...
Plasmodium lactate dehydrogenase (pLH) is one of the enzymes in glycolysis with potential target for chemotherapy. This study aimed to clone, overexpress and characterize soluble recombinant lactate dehydrogenase from in a bacterial system. Synthetic lactate dehydrogenase (-LDH) gene was cloned into pET21a expression vector, transformed into strain BL21 (DE3) expression system and then incubated for 18 h, 20 °C with the presence of 0.5 mM isopropyl β-d-thiogalactoside in Terrific broth supplemented with Magnesium sulfate, followed by protein purifications using Immobilized Metal Ion Affinity Chromatography and size exclusion chromatography (SEC). Enzymatic assay was conducted to determine the activity of the enzyme. SDS-PAGE analysis revealed that protein of 34 kDa size was present in the soluble fraction. In SEC, a single peak corresponding to the size of -LDH protein was observed, indicating that the protein has been successfully purified. From MALDI-TOF analysis findings, a peptide score of 282 was established, which is significant for lactate dehydrogenase from revealed via MASCOT analysis. Secondary structure analysis of CD spectra indicated 79.4% α helix and 1.37% β strand structure. Specific activity of recombinant -LDH was found to be 475.6 U/mg, confirming the presence of active protein. Soluble -LDH that is biologically active was produced, which can be used further in other malaria studies.
Topics: Antimalarials; L-Lactate Dehydrogenase; Malaria; Plasmodium knowlesi
PubMed: 34771034
DOI: 10.3390/molecules26216625 -
Chemical Biology & Drug Design Apr 2007Lactate dehydrogenase is an enzyme that catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD(+). Lactate dehydrogenase...
Lactate dehydrogenase is an enzyme that catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD(+). Lactate dehydrogenase is present at high levels in humans and Plasmodium spp. However, the function of lactate dehydrogenase in malarial infection is not well characterized. In this investigation, a new gene ontology technology is used to predict molecular function and biological pathways of lactate dehydrogenase. In comparison with human lactate dehydrogenase, the P. falciparum lactate dehydrogenase has similar molecular functions such as L-lactate dehydrogenase activity. Furthermore, P. falciparum lactate dehydrogenase has L-malate dehydrogenase activity. Although the amino acid sequences for human and P. falciparum lactate dehydrogenase are very different, the molecular functions are similar. This suggests that any non-selective therapeutic treatment aimed at blocking P. falciparum lactate dehydrogenase function may affect human lactate dehydrogenase. In contrast, a selective lactate dehydrogenase inhibitor targeting the l-malate dehydrogenase function of P. falciparum and its corresponding tricarboxylic acid cycle provides an attractive therapeutic opportunity.
Topics: Amino Acid Sequence; Animals; Antimalarials; Drug Design; Humans; L-Lactate Dehydrogenase; Molecular Sequence Data; Plasmodium falciparum; Sequence Alignment
PubMed: 17461976
DOI: 10.1111/j.1747-0285.2007.00495.x -
Veterinary and Comparative Oncology Dec 2009Lactate dehydrogenase (LDH) is commonly used in human cancer patients for prognostic purposes. Aim of this study was to determine the magnitude of serum LDH elevation in...
Lactate dehydrogenase (LDH) is commonly used in human cancer patients for prognostic purposes. Aim of this study was to determine the magnitude of serum LDH elevation in dogs with cancer compared with healthy dogs and dogs with non-neoplastic disease, and to verify whether it may support the diagnosis of specific malignancies. About 128 healthy dogs, 211 diseased dogs and 188 cancer dogs were enrolled. Dogs with cancer had significantly higher LDH than diseased (P < 0.001) and healthy dogs (P < 0.001), but large overlap was found. Dogs with lymphoma showed significantly higher LDH compared with dogs with carcinoma (P < 0.001) or mast cell tumour (MCT; P < 0.05) but not compared with other malignancies. When considering lymphoma and MCT, LDH levels were not different between early and advanced clinical stages. Measuring LDH levels may not be useful as a screening tool for cancer detection. More studies are needed to define its role in specific tumours.
Topics: Animals; Biomarkers, Tumor; Dog Diseases; Dogs; L-Lactate Dehydrogenase; Male; Neoplasms
PubMed: 19891694
DOI: 10.1111/j.1476-5829.2009.00196.x -
Structure (London, England : 1993) Dec 2023NADH-dependent d-lactate dehydrogenases (d-LDH) are important for the industrial production of d-lactic acid. Here, we identify and characterize an improved d-lactate...
NADH-dependent d-lactate dehydrogenases (d-LDH) are important for the industrial production of d-lactic acid. Here, we identify and characterize an improved d-lactate dehydrogenase mutant (d-LDH1) that contains the Pro101Gln mutation. The specific enzyme activities of d-LDH1 toward pyruvate and NADH are 21.8- and 11.0-fold greater compared to the wild-type enzyme. We determined the crystal structure of Apo-d-LDH1 at 2.65 Å resolution. Based on our structural analysis and docking studies, we explain the differences in activity with an altered binding conformation of NADH in d-LDH1. The role of the conserved residue Pro101 in d-LDH was further probed in site-directed mutagenesis experiments. We introduced d-LDH1 into Bacillus licheniformis yielding a d-lactic acid production of 145.9 g L within 60 h at 50°C, which was three times higher than that of the wild-type enzyme. The discovery of d-LDH1 will pave the way for the efficient production of d-lactic acid by thermophilic bacteria.
Topics: L-Lactate Dehydrogenase; NAD; Mutation; Lactic Acid
PubMed: 37729918
DOI: 10.1016/j.str.2023.08.019 -
Biochimica Et Biophysica Acta May 1966
Topics: Animals; Cattle; Cell Differentiation; Culture Techniques; Electrophoresis; Isoenzymes; L-Lactate Dehydrogenase; Lens, Crystalline; Pyruvates
PubMed: 5956951
DOI: 10.1016/0304-4165(66)90349-7 -
Archives of Oral Biology Feb 1972
Topics: Electrophoresis, Disc; Gingiva; Gingivitis; Histocytochemistry; Humans; Isoenzymes; L-Lactate Dehydrogenase; Spectrophotometry
PubMed: 4502057
DOI: 10.1016/0003-9969(72)90224-5 -
The American Review of Respiratory... Sep 1973
Topics: Agar; Electrophoresis; Gels; Humans; Isoenzymes; L-Lactate Dehydrogenase; Pleural Effusion
PubMed: 4745262
DOI: 10.1164/arrd.1973.108.3.660 -
Clinical Chemistry Jul 1976Human lactate dehydrogenase isoenzymes I and V have decreased activities when the reaction is initiated with lactate. No loss in lactate dehydrogenase I activity was...
Human lactate dehydrogenase isoenzymes I and V have decreased activities when the reaction is initiated with lactate. No loss in lactate dehydrogenase I activity was found when the reaction was initiated with enzyme or NAD+. For lactate dehydrogenase V an NAD+-initiated reaction, as compared to an enzyme-initiated reaction, yields lower activity in sodium pyrophosphate buffer but higher activity in tris(hydroxymethyl)aminomethane buffer. Both isoenzymes have higher lactate-to-pyruvate activity when assayed in the latter buffer than when assayed in the former. Human lactate dehydrogenase V (but not I) exhibited different activities when assayed with lactate from two different commercial sources. Human lactate dehydrogenase assayed by the pyruvate-to-lactate reaction is not affected by the choice of reaction initiator.
Topics: Humans; Isoenzymes; Kinetics; L-Lactate Dehydrogenase; Lactates; Methods; NAD
PubMed: 179734
DOI: No ID Found