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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The urf13TW gene, which is derived from the mitochondrial T-urf13 gene responsible for Texas cytoplasmic male sterility in maize, was expressed in Saccharomyces cerevisiae by targeting its translation product into mitochondria. Analysis by oxygraphy at the population level revealed that in the presence of methomyl the oxygen uptake of intact yeast cells carrying the targeted protein is strongly stimulated only with ethanol as respiratory substrate and not with glycerol, lactate, pyruvate, or acetate. When malate is the substrate oxidized by isolated mitochondria, interaction between the targeted protein and methomyl results in significant inhibition of oxygen uptake. This inhibition is eliminated and oxygen uptake is stimulated by subsequent addition of NAD+. Using 3,3'-dihexyloxacarbocyanine iodide [DiOC6(3)] as probe, interactive laser scanning and flow cytometry, which permit analysis at the individual cell level, demonstrated that specific staining of the mitochondrial compartment is obtained and that DiOC6(3) fluorescence serves as a measure of the membrane potential. Finally, it was shown that, as in T cytoplasm maize mitochondria, HmT toxin and methomyl dissipate the membrane potential of yeast mitochondria that carry the foreign protein. Furthermore, the results suggest that the HmT toxin and methomyl response is related to the plasmid copy number per cell and that the deleterious effect induced by HmT toxin is stronger than that of methomyl.
Mol Gen Genet 1993 Jan
PMID:Mitochondrial dysfunction in yeast expressing the cytoplasmic male sterility T-urf13 gene from maize: analysis at the population and individual cell level. 767 74

Lactate dehydrogenase was purified from testes of Uromastix hardwickii. The enzyme did not bind to DEAE-Sepharose at pH 7.2. A gel electrophoretic study of the crude enzyme showed the presence of three isoenzymes. The pH optima for pyruvate reduction and lactate oxidation were 7.0 and 9.5, respectively. The purified enzyme showed a single band after SDS-PAGE corresponding to a molecular weight of 34 KDa. The Km values for pyruvate, NADH, lactate and NAD+ were 0.019, 0.045, 9.0 and 0.011 mM, respectively. Pre-heating of the enzyme showed that it was stable up to 70 degrees C.
Biochem Mol Biol Int 1994 Nov
PMID:The isoenzyme forms of lactate dehydrogenase from the testes of Uromastix hardwickii. 770 13

This review is an exhaustive description of the biochemistry and enzymology of all 17 known NAD(P)(+)-amino acid dehydrogenases. These enzymes catalyze the oxidative deamination of an amino acid to its keto acid and ammonia, with the concomitant reduction of either NAD+ or NADP+. These enzymes have many important applications in industrial and medical settings and have been the object of prodigious enzymological research. This article describes all that is known about the poorly characterized members of the family and contains detailed information on the better characterized enzymes, including valine, phenylalanine, leucine, alanine, and glutamate dehydrogenases. The latter three enzymes have been the subject of extensive enzymological experimentation, and, consequently, their chemical mechanisms are discussed. The three-dimensional structure of the Clostridium symbiosum glutamate dehydrogenase has been determined recently and remains the only structure known of any amino acid dehydrogenase. The three-dimensional structure and its implications to the chemical mechanisms and rate-limiting steps of the amino acid dehydrogenase family are discussed.
Crit Rev Biochem Mol Biol 1994
PMID:The biochemistry and enzymology of amino acid dehydrogenases. 770 1

The effects of alloxan diabetes and its reversal with insulin treatment, on NADH-oxidase (E.C.1.6.99.3) was measured in the microsomal fractions of brain, liver and kidney at different time interval after diabetes induction. A significant increase was found in the enzyme activity in brain and kidney microsomes of the diabetic animals, whereas liver showed a decrease. The decrease in the NAD+/NADH ratio in the diabetes reported earlier could be due to the changes in the enzyme activity as well as other changes in the metabolite concentration.
Biochem Mol Biol Int 1994 Nov
PMID:Changes in the activity of NADH-oxidase in rat tissues during experimental diabetes. 772

The effects of the cytosolic and mitochondrial redox state on the function and phosphorylation potential of working perfused rabbit hearts were studied. Hearts were perfused with glucose, while lactate, aminooxy-acetate (an inhibitor of the malate-aspartate shuttle), beta-hydroxybutyrate, and pyruvate were sequentially added to the perfusate to manipulate the cytosolic and mitochondrial NAD+/NADH ratio. The phosphorylation potential and product of ADP and P(i) were both found to be proportional to mitochondrial redox state. There was no overall relationship between cytosolic redox potential and the ATP/ADP x P(i) ratio, although at high mitochondrial NADH, there was a tendency for the states with more reduced cytoplasm to be associated with a lower phosphorylation potential. Cardiac output and dP/dt were decreased after 75 microM aminooxy-acetate was present for 15 min, and remained low when 0.5-1.0 mM beta-hydroxybutyrate was added, even though the beta-hydroxybutyrate period was characterized by both very low cytosolic NAD+/NADH and high mitochondrial NADH. Function returned to normal when the cytoplasm was oxidized by addition of 10 mM pyruvate, and although MVO2 rose from 4.0 +/- 0.4 to 5.0 +/- 0.5, this was not accompanied by statistical changes in either mitochondrial NADH or phosphorylation potential. Therefore, the cytosolic redox state may play a role in cardiac function, but has only a minor contribution to the regulation of the phosphorylation potential in the working perfused rabbit heart.
J Mol Cell Cardiol 1994 Dec
PMID:The relationship between phosphorylation potential and redox state in the isolated working rabbit heart. 773 Oct 48

Bovine liver dihydrodiol dehydrogenase (DD2) was inactivated following pseudo-first order manner by the treatment of 5 mM 2,3-butanedione (BD) as functions of incubation-time and concentration. Anionic substrates or analog which have a carboxyl group, D-glucuronate, p-carboxybenzaldehyde and D-glycerate, protected DD2 efficiently. But, the other substrates or coenzymes and their analogs did not show any protection on the inactivation, i.e., D,L-glyceraldehyde, D-erythrose, NADP+, NAD+, 2',5'-ADP, 2'-AMP. Results of kinetic analyses suggest that the inactivated enzyme lost its binding ability to anionic substrates. The inactivated enzyme was reactivated very effectively by removing excess BD by gelfiltration for 30 min.
Biochem Mol Biol Int 1995 Jan
PMID:Role of arginine residues of bovine liver dihydrodiol dehydrogenase 2 in the binding of anionic substrates. 773 34

Lactate dehydrogenase isoenzyme-1 was purified from liver of Uromastix hardwickii using colchicine-Sepharose and heat-inactivation methods. The crude enzyme showed four isoenzymes by agarose gel electrophoresis (AGE). The purified enzyme showed a single band after native AGE and SDS-PAGE corresponding to a molecular weight of 34 kDa. The enzyme did not bind with DEAE-Sepharose at pH 7.2. The optimum pH for forward reaction was 7.5, while for reverse reaction, the maximum activity was at pH 9.5. The Km values for pyruvate, NADH, lactate and NAD+ were 0.105, 0.045, 9.0 and 0.011 mM, respectively. The pyruvate showed maximum activity at about 150 microM and then starts showing inhibition at higher concentration. Pre-heating of enzyme showed that it was stable at 80 degrees C for 30 min and at 100 degrees C it became inactive immediately. Oxalate, glutamate, Cu2+, Co2+, Mn2+, and Mg2+ have shown inhibitory effects both for forward- and reverse-reactions. From these properties, we suggest that LDH-1 from Uromastix liver may be quite different from that of other vertebrates.
Comp Biochem Physiol B Biochem Mol Biol 1995 May
PMID:Purification and properties of lactate dehydrogenase from liver of Uromastix hardwickii. 774 34

The mitochondrial NADH/NAD+ ratio for free nucleotides in rat pancreatic islets was judged from the cell content in L-glutamate and L-alanine, 2-ketoglutarate and pyruvate, and NH4+. At a physiological concentration of D-glucose, such a ratio averaged 9.6 +/- 1.1%. A rise in hexose concentrations, above a threshold value in excess of 5.6 mM, caused a rapid, sustained and rapidly reversible decrease in the mitochondrial NADH/NAD+ ratio. It is speculated that in the process of glucose-stimulated insulin release, the latter change participates in the coupling between metabolic and secretory events by favouring both the activity of key mitochondrial dehydrogenases and the translocation of Ca2+ from the mitochondria into the cytosol.
Mol Cell Biochem 1995 Jan 12
PMID:Hexose metabolism in pancreatic islets: effect of D-glucose on the mitochondrial redox state. 775 41

Poly(ADP-ribosyl)ation is a posttranslational modification of nuclear proteins catalyzed by poly(ADP-ribose) polymerase (PARP; EC 2.4.2.30), with NAD+ serving as the substrate. PARP is strongly activated upon recognition of DNA strand breaks by its DNA-binding domain. Experiments with low-molecular-weight inhibitors of PARP have led to the view that PARP activity plays a role in DNA repair and possibly also in DNA replication, cell proliferation, and differentiation. Accumulating evidence for nonspecific inhibitor effects prompted us to develop a molecular genetic system to inhibit PARP in living cells, i.e., to overexpress selectively the DNA-binding domain of PARP as a dominant negative mutant. Here we report on a cell culture system which allows inducible, high-level expression of the DNA-binding domain. Induction of this domain leads to about 90% reduction of poly(ADP-ribose) accumulation after gamma-irradiation and sensitizes cells to the cytotoxic effect of gamma-irradiation and of N-methyl-N'-nitro-N-nitrosoguanidine. In contrast, induction does not affect normal cellular proliferation or the replication of a transfected polyomavirus replicon. Thus, trans-dominant inhibition of the poly(ADP-ribose) accumulation occurring after gamma-irradiation or N-methyl-N'-nitro-N-nitrosoguanidine is specifically associated with a disturbance of the cellular recovery from the inflicted damage.
Mol Cell Biol 1995 Jun
PMID:trans-dominant inhibition of poly(ADP-ribosyl)ation sensitizes cells against gamma-irradiation and N-methyl-N'-nitro-N-nitrosoguanidine but does not limit DNA replication of a polyomavirus replicon. 776 Aug 11

Metabolic control analysis allows one to express the elasticity coefficients (which describe the "local" kinetic features of enzymes) in terms of the control coefficients (quantitative indicators of the "global" control properties). However, when coenzymes (or metabolites linked by conservation constraints) are present in the pathway this procedure yields the "apparent" values of elasticity coefficients that correspond to the kinetic responses of the enzymes to such a simultaneous change of the coenzyme forms which leaves the total concentration of these forms unchanged (e.g., NAD+ + NADH in the glycolysis). We show that a generalised connectivity theorem (Kholodenko et al, Eur. J. Biochem. (1994) 225, 179-186) makes it possible to express the elasticity coefficients with respect to every coenzyme form separately. Such expressions include (i) the control coefficients and (ii) the responses to changes in the total concentrations of the coenzymes.
Biochem Mol Biol Int 1995 Mar
PMID:Coenzyme cycles and metabolic control analysis: the determination of the elasticity coefficients from the generalised connectivity theorem. 777 96


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