Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.28 (lactic acid dehydrogenase)
 476 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1) In intact Ehrlich ascites tumour cells the anaerobic glycolytic flux rate and pattern of intermediates have been investigated at different pH values of the extracellular medium. 2) As predicted from the dependence of the lactic acid dehydrogenase equilibrium on pH a strong negative correlation between log ([lactate]/[pyruvate]) and pH has been found. 3) The steady state fluxes of glycolysis at pH 8.0 and 7.4 are rather equal, despite significant differences in the intracellular concentrations of glycolytic intermediates. At pH 8.0 the concentrations of ATP, glucose 6-phosphate, and fructose 6-phosphate are lower, and the concentrations of ADP, AMP, fructose 1,6-bisphosphate, triose phosphates, phosphoglycerates, and phosphoenolpyruvate are higher than at pH 7.4. 4) From the analysis of the pH dependent changes of metabolites it follows that different mechanisms are responsible for maintaining equal actual activities of hexokinase, phosphofructokinase and pyruvate kinase at pH 7.4 and 8.0. 5) From an application of the linear theory of enzymatic chains and a calculation of the control strength of the regulatory important enzymes results that hexokinase is evidently rate-limiting for glycolysis, and phosphofructokinase is also significantly influencing the glycolytic flux. Pyruvate kinase and glyceraldehyde phosphate dehydrogenase, on the other hand, do not significantly affect the rate of the overall glycolytic flux in ascites.
 ...
PMID:Regulation of anaerobic glycolysis in Ehrlich ascites tumour cells. 2 29

In Peptostreptococcus elsdenii, a three-component flavoprotein electron transfer system catalyzes the oxidation of lactate and the reduction of crotonyl-coenzyme A (CoA). Spectral evidence showed that D-lactate dehydrogenase, when reduced by D-lactate, was able to reduce butyryl-CoA dehydrogenase, but only in the presence of the electron-transferring flavoprotein. Reduced nicotinamide adenine dinucleotide could replace reduced D-lactate dehydrogenase. A reconstituted system, containing the three partially purified enzymes, excess D-lactate, and a limiting amount of crotonyl-CoA, reduced the crotonyl-CoA to butyryl-CoA, but only if all components were present. The electron-transferring flavoprotein activity, purified 22-fold, was separated into two major flavoprotein components, A and B, after polyacrylamide gel electrophoresis. Elution of the proteins and subsequent kinetic assays of the eluates showed that component B catalyzes the reduction of butyryl-CoA dehydrogenase by reduced D-lactate dehydrogenase, whereas component A does not. Both A and B catalyzed the reduction of butyryl-CoA dehydrogenase by reduced nicotinamide adenine dinucleotide. The results suggest that the D-lactate dehydrogenase-dependent reduction involves a heretofore unrecognized component of the electron-transferring protein group which may utilize an unusual flavin, 6-hydroxy-7,8-dimethyl-10-(ribityl-5'-adenosine diphosphate)-isoalloxazine.
 ...
PMID:Electron-transferring flavoprotein of Peptostreptococcus elsdenii that functions in the reduction of acrylyl-coenzyme A. 17 88

A chronic animal experiment was designed to examine the changes in blood components induced by the use of a centrifugal pump (CP). In the pump, an impeller spins in a blood chamber by magnetic coupling with a rotating magnet outside the blood chamber. A pulsatile ventricular assist device was implanted between the left atrium and the descending aorta in four goats weighing from 63 to 75 kg; the CP was installed to replace the assist device, without surgery and anesthesia, more than 2 weeks later when the influences of implantation surgery were diminished. Antithrombotic therapy was performed with oral administration of an antiplatelet agent, cilostazol, a cyclic adenosine monophosphate phosphodiesterase at a dose of 30 mg/kg/day. No significant differences were observed in any of the following parameters: 1) hematocrit, 2) plasma free hemoglobin, 3) lactic acid dehydrogenase, 4) adenosine diphosphate, 5) platelet count, 6) fibrinogen, and 7) antithrombin III, between the data before and after the use of the CP, nor were deformation or pseudopods of platelets seen. The CP developed in the authors' institute and evaluated in this study did not damage blood components, and it proved to be a promising device for long-term use.
 ...
PMID:Influence of an impeller centrifugal pump on blood components in chronic animal experiments. 145 25

The NAD-dependent D-lactate dehydrogenase from Lactobacillus bulgaricus has been purified to homogeneity. This enzyme was a dimer made of two identical chains of molecular mass 37,000. Saturation by either substrate was hyperbolic, with Km values of 50 microM for NADH and 1 mM for pyruvate. The specific activity was 2200 units/mg and was not affected by the presence of fructose-1,6-bisphosphate, Mn2+ ions, ATP or ADP. The amino-terminal sequence determined on 50 residues showed no significant homology with known lactate dehydrogenases, suggesting that the D-lactate dehydrogenase from L. bulgaricus could not be evolutionarily related to the family of NAD-dependent L-lactate dehydrogenases.
 ...
PMID:Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: a possible different evolutionary origin for the D- and L-lactate dehydrogenases. 204 42

Chinese hamster ovary (CHO-K1) cells were pulse labeled with [3H]serine, and the synthesis of phosphatidyl[3H]ethanolamine from phosphatidyl[3H]serine during the subsequent chase was used as a measure of lipid translocation to the mitochondria. When the CHO-K1 cells were pulse labeled and subsequently permeabilized with 50 micrograms of saponin per ml, there was no significant turnover of nascent phosphatidyl[3H]serine to form phosphatidyl[3H]ethanolamine during an ensuing chase. Saponin treatment rendered greater than 99% of the cells permeable as judged by trypan blue exclusion and depleted them of 85% of their complement of cytosolic proteins as determined by residual lactic acid dehydrogenase activity. Supplementation of the permeabilized cells with 2 mM ATP resulted in significant phosphatidyl[3H]ethanolamine synthesis (83% of that found in intact cells) from phosphatidyl[3H]serine during a subsequent 2-hr chase. Phosphatidyl[3H]ethanolamine synthesis essentially ceased after 2 hr in the permeabilized cells. The translocation-dependent synthesis of phosphatidyl[3H]ethanolamine was a saturable process with respect to ATP concentration in permeabilized cells. The conversion of phosphatidyl[3H]serine to phosphatidyl[3H]ethanolamine did not occur in saponin-treated cultures supplemented with 2 mM AMP, 2 mM 5'-adenylyl imidodiphosphate, or apyrase (2.5 units/ml) plus 2 mM ATP. ATP was the most effective nucleotide, but the addition of GTP, CTP, UTP, and ADP also supported the translocation-dependent synthesis of phosphatidyl[3H]ethanolamine albeit to a lesser extent. These data provide evidence that the interorganelle translocation of phosphatidylserine requires ATP and is largely independent of soluble cytosolic proteins.
 ...
PMID:Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells. 260 82

The Escherichia coli open reading frame YbdK encodes a member of a large bacterial protein family of unknown biological function. The sequences within this family are remotely related to the sequence of gamma-glutamate-cysteine ligase (gamma-GCS), an enzyme in the glutathione biosynthetic pathway. A gene encoding gamma-GCS in E. coli is already known. The 2.15 A resolution crystal structure of YbdK reveals an overall fold similar to that of glutamine synthetase (GS), a nitrogen metabolism enzyme that ligates glutamate and ammonia to yield glutamine. GS and gamma-GCS perform related chemical reactions and require ATP and Mg2+ for their activity. The Mg2+-dependent binding of ATP to YbdK was confirmed by fluorescence spectroscopy employing 2'(or 3')-O-(trinitrophenyl)adenosine 5'-triphosphate, and yielding a dissociation constant of 3 +/- 0.5 microM. The structure of YbdK contains a crevice that corresponds to the binding sites of ATP, Mg2+ and glutamate in GS. Many of the GS residues that coordinate the metal ions and interact with glutamic acid and the phosphoryl and ribosyl groups of ATP are also present in YbdK. GS amino acids that have been associated with ammonia binding have no obvious counterparts in YbdK, consistent with a substrate specificity that is different from that of GS. Ligase activity between glutamic acid and each of the twenty amino acid residues was tested on high performance liquid chromatography (HPLC) by following the hydrolysis of ATP to ADP. Catalysis was observed only with cysteine. A pyruvate kinase/lactic acid dehydrogenase coupled assay was used to rule out GS activity and to determine that YbdK exhibits gamma-GCS activity. The catalytic rate was found to be approximately 500-fold slower than that reported for authentic gamma-GCS.
 ...
PMID:YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays. 1521 20