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Advances in Enzymology and Related... 1973
Review
Topics: Amino Acid Sequence; Amino Acids; Animals; Bacteria; Binding Sites; Biological Evolution; Chemical Phenomena; Chemistry; Genetics; Isoenzymes; Kinetics; L-Lactate Dehydrogenase; Macromolecular Substances; Models, Chemical; Models, Structural; Molecular Weight; NAD; NADP; Oxidation-Reduction; Plants; Protein Binding; Protein Conformation; Protein Denaturation; Species Specificity; Structure-Activity Relationship
PubMed: 4144036
DOI: 10.1002/9780470122822.ch2 -
Biotechnology and Applied Biochemistry Oct 1986D-(+)-Lactate dehydrogenase from Lactobacillus murinus was purified 670-fold. The Mr was 140,000 as determined by gel filtration. Maximum enzymatic activity was observed...
D-(+)-Lactate dehydrogenase from Lactobacillus murinus was purified 670-fold. The Mr was 140,000 as determined by gel filtration. Maximum enzymatic activity was observed at 25 degrees C and pH 6.0 in 200 mM Na2KPO4 buffer. When the temperature was increased from 60 to 65 degrees C, the enzyme was completely inactive in 5 min. The apparent Km for pyruvate and NADH were 4.7 x 10(-4) and 1 x 10(-5) M, respectively. Pyruvate analogs such as oxalate, oxamate, 2-oxobutyrate, and malonate acted as a competitive inhibitors. L-Lactate and L-malate were noncompetitive inhibitors.
Topics: Bacterial Proteins; Hot Temperature; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Lactobacillus; Substrate Specificity
PubMed: 3768146
DOI: No ID Found -
Molecular Biology and Evolution Jun 2003Vertebrate eye lenses mostly contain two abundant types of proteins, the alpha-crystallins and the beta/gamma-crystallins. In addition, certain housekeeping enzymes are...
Vertebrate eye lenses mostly contain two abundant types of proteins, the alpha-crystallins and the beta/gamma-crystallins. In addition, certain housekeeping enzymes are highly expressed as crystallins in various taxa. We now observed an unusual approximately 41-kd protein that makes up 16% to 18% of the total protein in the platypus eye lens. Its cDNA sequence was determined, which identified the protein as muscle-type lactate dehydrogenase A (LDH-A). It is the first observation of LDH-A as a crystallin, and we designate it upsilon (upsilon)-crystallin. Interestingly, the related heart-type LDH-B occurs as an abundant lens protein, known as epsilon-crystallin, in many birds and crocodiles. Thus, two members of the ldh gene family have independently been recruited as crystallins in different higher vertebrate lineages, suggesting that they are particularly suited for this purpose in terms of gene regulatory or protein structural properties. To establish whether platypus LDH-A/upsilon-crystallin has been under different selective constraints as compared with other vertebrate LDH-A sequences, we reconstructed the vertebrate ldh-a gene phylogeny. No conspicuous rate deviations or amino acid replacements were observed.
Topics: Amino Acid Sequence; Animals; Base Sequence; Crystallins; DNA Primers; Electrophoresis, Polyacrylamide Gel; Isoenzymes; L-Lactate Dehydrogenase; Lactate Dehydrogenase 5; Male; Molecular Sequence Data; Platypus; Sequence Homology, Amino Acid
PubMed: 12716980
DOI: 10.1093/molbev/msg116 -
Bioscience, Biotechnology, and... 2014Studies indicated that lactate dehydrogenase C4 (LDH-C4) was a good target protein for development of contraceptive drugs. Virtual screening and in vitro enzyme assay...
Studies indicated that lactate dehydrogenase C4 (LDH-C4) was a good target protein for development of contraceptive drugs. Virtual screening and in vitro enzyme assay using pika LDH-C4 as target protein revealed NSC61610, NSC215718, and NSC345647 with Ki of 7.8, 27, and 41 μM separately. This study might be helpful for development of pika contraceptive drugs.
Topics: Animals; Catalytic Domain; China; Drug Evaluation, Preclinical; Enzyme Inhibitors; Isoenzymes; L-Lactate Dehydrogenase; Lagomorpha; Molecular Docking Simulation
PubMed: 25036963
DOI: 10.1080/09168451.2014.890038 -
The Biochemical Journal Jan 19691. Human foetal skeletal muscles involved in support and in periodic contractility were studied for their content of total extractable lactate dehydrogenase, glucose...
1. Human foetal skeletal muscles involved in support and in periodic contractility were studied for their content of total extractable lactate dehydrogenase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities as well as for the relative distribution of lactate dehydrogenase isoenzymes. 2. During foetal development a linear steady increase in total lactate dehydrogenase activity as well as a linear decrease in the H/M sub-unit ratio of the isoenzymes was found. 3. No significant changes were found in the activities of the enzymes of the hexose monophosphate shunt (C-6 oxidation). 4. The changes found suggest a steady increased synthesis of lactate dehydrogenase M-sub-units in human skeletal muscles during foetal development. 5. The weekly changes in the total lactate dehydrogenase activity and in lactate dehydrogenase isoenzymes are lower in muscles involved in support than in those involved in periodic contractility. 6. These findings, together with the literature available, are consistent with the morphological fact that foetal development of skeletal muscles mostly concerns the white muscle fibres and not the red muscle fibres.
Topics: Female; Fetus; Glucosephosphate Dehydrogenase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Muscles; Phosphogluconate Dehydrogenase; Pregnancy
PubMed: 5812626
DOI: 10.1042/bj1110219 -
Postgraduate Medicine Jun 1973
Topics: Anemia, Hemolytic; Electrophoresis; Hepatitis; Humans; Isoenzymes; Kidney Diseases; L-Lactate Dehydrogenase; Myocardial Infarction; Necrosis
PubMed: 4707883
DOI: 10.1080/00325481.1973.11713493 -
Archives of Biochemistry and Biophysics Apr 2024d-lactate dehydrogenases are known to be expressed by prokaryotes and by eukaryotic invertebrates, and over the years the functional and structural features of some...
d-lactate dehydrogenases are known to be expressed by prokaryotes and by eukaryotic invertebrates, and over the years the functional and structural features of some bacterial representatives of this enzyme ensemble have been investigated quite in detail. Remarkably, a human gene coding for a putative d-lactate dehydrogenase (DLDH) was identified and characterized, disclosing the occurrence of alternative splicing of its primary transcript. This translates into the expression of two human DLDH (hDLDH) isoforms, the molecular mass of which is expected to differ by 2.7 kDa. However, no information on these two hDLDH isoforms is available at the protein level. Here we report on the catalytic action of these enzymes, along with a first analysis of their structural features. In particular, we show that hDLDH is strictly stereospecific, with the larger isoform (hDLDH-1) featuring higher activity at the expense of d-lactate when compared to its smaller counterpart (hDLDH-2). Furthermore, we found that hDLDH is strongly inhibited by oxalate, as indicated by a K equal to 1.2 μM for this dicarboxylic acid. Structurally speaking, hDLDH-1 and hDLDH-2 were determined, by means of gel filtration and dynamic light scattering experiments, to be a hexamer and a tetramer, respectively. Moreover, in agreement with previous studies performed with human mitochondria, we identified FAD as the cofactor of hDLDH, and we report here a model of FAD binding by the human d-lactate dehydrogenase. Interestingly, the mutations W323C and T412 M negatively affect the activity of hDLDH, most likely by impairing the enzyme electron-acceptor site.
Topics: Humans; L-Lactate Dehydrogenase; Lactic Acid; Oxalates; Protein Isoforms; Mutation; Lactate Dehydrogenases
PubMed: 38373542
DOI: 10.1016/j.abb.2024.109932 -
Biochemical and Biophysical Research... Jul 2017Although pig represents a model species in biomedical research including studies dealing with liver patho-physiology, some aspects of liver metabolism need to be...
Although pig represents a model species in biomedical research including studies dealing with liver patho-physiology, some aspects of liver metabolism need to be addressed. In particular, whether and how pig mitochondria can metabolize l-lactate remains to be established. We show here that pig liver mitochondria (PLM) possess their own l-lactate dehydrogenase (mL-LDH). This was shown both via immunological analysis and by assaying photometrically the L-LDH reaction in solubilised PLM. The mL-LDH reaction shows hyperbolic dependence on the substrate concentration, it is inhibited by oxamate and proves to differ from the cytosolic activity (cL-LDH), as revealed by the difference found in both pH profiles and temperature dependence of m- and cL-LDH. Titration experiments with digitonin show that mL-LDH is restricted in mitochondrial inner compartment. In agreement with the above findings, three genes in Sus scrofa genome encoded for L-LDH subunits which are predicted to have mitochondrial localization, as investigated by Target P 1.1 and PredSL analysis.
Topics: Animals; Enzyme Inhibitors; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Liver; Mitochondria, Liver; Organic Chemicals; Structure-Activity Relationship; Swine; Temperature
PubMed: 28564593
DOI: 10.1016/j.bbrc.2017.05.154 -
Journal of Periodontal Research 1971
Topics: Electrophoresis; Humans; Isoenzymes; L-Lactate Dehydrogenase; Periodontium
PubMed: 4255221
DOI: 10.1111/j.1600-0765.1971.tb00599.x -
Clinica Chimica Acta; International... May 2017
Topics: Aged; Female; Humans; L-Lactate Dehydrogenase; Neuraminidase; Paraproteins
PubMed: 28300541
DOI: 10.1016/j.cca.2017.03.011