Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.37 (malate dehydrogenase)
4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Purified pea chloroplast NADP-malate dehydrogenase (S)-malate: NADP+ oxidoreductase, EC 1.1.1.82) was digested with trypsin and the resulting peptides were separated by HPLC and sequenced. Together with the information from earlier work (Fickenscher, K. et al. (1987) Eur. J. Biochem. 168, 653-658) the total sequence is not known to an extent of 78%. Comparison with the sequence of the corn NADP-malate dehydrogenase deduced from its cDNA (Metzler, M.C. et al. (1989) Plant Mol. Biol. 12, 713-722) showed 84% agreement; however, the 11 N-terminal residues exhibit only 27% similarity. The N- and C-terminal extrapeptides of the pea NADP-malate dehydrogenase when aligned with non-regulatory NAD-malate dehydrogenases from bacteria or mammals consist of 30 and 17 amino acids, respectively. Since all cysteine-containing peptides were sequenced, the number of eight cysteines per subunit of the pea enzyme was established. The native, oxidized enzyme is characterized by an extremely slow reactivity of two thiols. Titration of the thiols of the denatured, oxidized enzyme both with DTNB and with pCMB resulted in six thiols not involved in disulfide formation. Therefore, one disulfide bridge must be present per 38.9 kDa subunit. Analysis of disulfide bonds by urea gel electrophoresis confirmed this finding. Using digestion products of NADP-malate dehydrogenase with aminopeptidase K, the location of the single disulfide bridge was established to be on the N-terminal arm (Cys-12 and Cys-17) of the polypeptide chain.
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PMID:Primary structure and analysis of the location of the regulatory disulfide bond of pea chloroplast NADP-malate dehydrogenase. 198 82

Effects of gossypol on human spermatozoal enzymes were investigated. This compound was found to be a potent inhibitor of the NAD-linked enzymes, glucelaldehyde-3-phosphate dehydrogenase (GA3PDH), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), and isocitrate dehydrogenase (ICDH). MDH was inhibited by gossypol when the reaction was carried out in malate-oxalacetate (direct) or oxalacetate-malate (reverse) directions. The I50 of gossypol for the direct reaction was 2.9 microM, whereas that for the reverse reaction was 1.2 microM. Reciprocal plots due to Lineweaver-Burk showed that MDH is inhibited in a noncompetitive manner with respect to both reactions. LDH was also inhibited by this compound when pyruvate or alpha-ketobutyrate was used as a substrate. Gossypol was a noncompetitive inhibitor for LDH. The I50 of gossypol for LDH were 9.8 microM and 11.3 microM, when using pyruvate and alpha-ketobutyrate, respectively as substrates. The I50 of gossypol for GA3PDH and ICDH were 110 microM and 2.7 microM, respectively.
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PMID:Inhibition kinetics of NAD-linked enzymes by gossypol acetic acid. 207 51

Two carbon catabolite repression mutants of S. cerevisiae were isolated and characterized. In spite of the selection procedure (red colonies after tetrazolium overlay at high glucose concentration) the mutants exhibited a respiration which was as repressed as that of the parental strain or even more repressed. When grown at high glucose concentration the mutants display hyper-repression of cytochrome aa3 and of certain mitochondrial enzymes (L- and D-lactate dehydrogenases) but not of others (malate dehydrogenase, succinate dehydrogenase), indicating the existence of separate control sites for the different genes involved in the mitochondrial biogenesis. The data obtained pointed out that the same mutation affects both repression and derepression. In addition, the mutation(s) give rise to the complete derepression of the cytoplasmic enzyme NAD-glutamate dehydrogenase at 10% glucose whereas the enzyme is normally repressed at 3% glucose. The results of the genetic analysis indicate the mitochondrial nature of the mutation(s).
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PMID:Isolation and characterization of carbon catabolite repression mutants in Saccharomyces cerevisiae. 208 99

NAD dependent malate dehydrogenases of three trematode species, Notocotylus attenuatus, N. ephemera and N. imbricatus, have been investigated by electrophoresis. Seven different zones with 15 isoenzymes in N. attenuatus, 16 isoenzymes in N. ephemera and 11 isoenzymes in N. imbricatus have been found in MDH spectra. Isoenzymes of MDH are controlled by seven polymorphic loci. The activity of isoenzymes of three slowly migrating zones is 10 and more times higher than that of fast zones (4-7). The genotypes of adults in one strain are genetically identical, independent ot the development in different definitive hosts. The spectra of MDH of the investigated Notocotylus species are different in slowly migrating isoenzymes (1-3 zones).
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PMID:[Multiple forms of NAD-dependent malate dehydrogenase in 3 species of trematodes of the genus Notocotylus (Trematoda: Notocotylidae)]. 210 2

The activities of serum malate dehydrogenase (MDH) and its mitochondrial isoenzyme (MDHm) were studied in sera of patients with liver disease. They proved to be more useful than those of aspartate aminotransferase (AST) and its mitochondrial isoenzyme for detection of hepatocellular carcinoma and acute circulatory failure, and for estimation of the severity of acute hepatitis. The N/T value measuring system, which is adaptable for autoanalysis and allows simultaneous determination of activities depending on NAD and thionicotinamide adenine dinucleotide (thio-NAD), yields both the total activity of MDH and the N/T value which was correlated significantly with MDHm/MDH (r = 0.748). Assay of MDH and its mitochondrial isoenzyme in association with the N/T value measuring system seems to be more useful and less time consuming for estimation of the severity of liver diseases than that of AST and its mitochondrial isoenzyme.
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PMID:Clinical usefulness of malate dehydrogenase and its mitochondrial isoenzyme in comparison with aspartate aminotransferase and its mitochondrial isoenzyme in sera of patients with liver disease. 217 15

A simple plate-assay has been developed to screen microorganisms for L-malic acid production. Acid producing organisms were identified, after microbial colony growth on media containing glucose or fumaric acid as sole carbons sources, by formation of a dark halo of formazan. The halo was observed when the plate was covered with a soft agar overlay containing NAD(+)-malate dehydrogenase, NAD+, phenazine methosulfate (PMS) and 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide (MTT). The assay developed is simple, specific for L-malic acid and therefore can be used to identify L-malic acid producing filamentous fungi using glucose as carbon source (e.g. Aspergillus strains). The assay is also applicable for screening bacteria with high fumarase activity, able to convert fumaric acid to L-malic acid.
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PMID:A simple plate-assay for the screening of L-malic acid producing microorganisms. 218 83

Mitochondrial NAD(H)-specific isocitrate dehydrogenase was purified from Saccharomyces cerevisiae for analyses of subunit structure and expression. Two subunits of the enzyme with different molecular weights (39,000 and 40,000) and slightly different isoelectric points were resolved by denaturing electrophoretic techniques. Sequence analysis of the purified subunits showed that the polypeptides have different amino termini. By using an antiserum to the native enzyme prepared in rabbits, subunit-specific immunoglobulin G fractions were obtained by affinity purification, indicating that the subunits are also immunochemically distinct. The levels of NAD(H)-specific isocitrate dehydrogenase activity and immunoreactivity were found to correlate closely with those of a second tricarboxylic acid cycle enzyme, malate dehydrogenase, in yeast cells grown under a variety of conditions. S. cerevisiae mutants with defects in NAD(H)-specific isocitrate dehydrogenase were identified by screening a collection of yeast mutants with acetate-negative growth phenotypes. Immunochemical assays were used to demonstrate that one mutant strain lacks the 40,000-molecular-weight subunit (IDH1) and that a second strain lacks the 39,000-molecular-weight subunit (IDH2). Mitochondria isolated from the IDH1 and IDH2 mutants exhibited a markedly reduced capacity for utilization of either isocitrate or citrate for respiratory O2 consumption. This confirms an essential role for NAD(H)-specific isocitrate dehydrogenase in oxidative functions in the tricarboxylic acid cycle.
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PMID:Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae. 219 51

Malate dehydrogenase (NADP) (NADP-MDH) is an important enzyme of the photosynthetic CO2 fixation pathway of C4 plants. We have isolated two clones from a sorghum lambda gt11 cDNA library (CM3, 932 bp, and CM7, 1441 bp). Nucleotide sequence analysis of the cDNAs CM3 and CM7 showed the existence of two NADP-MDH mRNA species encoding different enzyme subunits. Microsequencing of the N-terminus of the mature protein indicated that a specific cleavage of 13 amino acids occurred during the purification steps of the enzyme. The full-length cDNA CM7 contains a large open reading frame encoding an NH2-terminal transit peptide of 40 amino acids and a mature protein of 389 amino acids (42.207 kDa). Alignment of the NADP-MDH sequence with those of several malate dehydrogenases revealed some similarities with NAD-MDHs.
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PMID:Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD). 220 86

The NAD analog 3-acetylpyridine adenine nucleotide (APAD), because of its higher oxidation potential, has proven useful for the direct enzymatic measurement of such compounds as lactate, malate, glutamate, etc., for which the equilibrium with NAD+ as oxidant is unfavorable. An enzymatic cycling method which is capable of increasing the sensitivity of such reactions 10,000-fold or more is described. The APADH produced in the original stoichiometric reaction is used to catalyze a cycling reaction that employs lactate and malate dehydrogenases (EC 1.1.1.27 and EC 1.1.1.37) to generate (from lactate plus oxalacetate) very large quantities of pyruvate and malate. After the cycling step, the malate formed is measured with NAD+ and with malate dehydrogenase, plus aspartate aminotransferase, and oxaloacetate to pull this indicator reaction to completion. The application of this cycling method is illustrated by analysis of malate in the range 1 to 10 pmol.
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PMID:An enzymatic cycling method for 3-acetylpyridine adenine dinucleotide to increase the sensitivity of enzymatic methods which employ this NAD analog. 236 93

42 residues of the N-terminal amino acid sequence of malate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius have been determined as VKVAFIGVGRGVGQTIAYNTIVNGYADEVMLYDVVPELPTKK. In eubacterial and eukaryotic enzymes this region is known to encompass residues involved in pyridine nucleotide binding. In the archaebacterial enzyme the residues Gly-7, Gly-11 and Asp-33 are also present. The data suggest that in the enzyme from S. acidocaldarius like in the other malate dehydrogenases the binding domain for NAD(H) is localized at the N-terminal part of the polypeptide chain. The archaebacterial enzyme is homologous to the other malate dehydrogenases, of which the amino acid sequences are known, however, it is only distantly related to the mitochondrial/E. coli group and the cytosolic/Thermus flavus group.
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PMID:Archaebacterial malate dehydrogenase: the amino-terminal sequence of the enzyme from Sulfolobus acidocaldarius is homologous to the eubacterial and eukaryotic malate dehydrogenases. 249 31


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