Disease relevance of mdh

• Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica [1].
• Nucleotide sequences of the mdh gene encoding the metabolic enzyme malate dehydrogenase (MDH) were determined for 44 strains representing the major lineages of Escherichia coli and the eight subspecies of Salmonella enterica [1].
• Comparative analysis showed the nucleotide sequence to be very closely related to that determined for the Thermus flavus mdh gene and flanking regions, with no differences between the predicted amino acid sequences of the MDHs [2].
• Nicotinamide adenine dinucleotide-linked malate dehydrogenase has been purified from Pseudomonas testosteroni (ATCC 11996) [3].
• The only enzyme of the citric acid cycle for which no open reading frame (ORF) was found in the Helicobacter pylori genome is the NAD-dependent malate dehydrogenase [4].

High impact information on mdh

• But recombination at mdh has not occurred with sufficient frequency to obscure the phylogenetic relationships among strains indicated by multilocus enzyme electrophoresis, total DNA hybridization, and sequence analysis of the gapA and putP genes [1].
• The enzyme showed neither malate dehydrogenase nor lactate dehydrogenase activity but catalyzed the NADPH-dependent reduction of such cyclic imines as Delta(1)-piperideine-2-carboxylate and Delta(1)-pyrroline-2-carboxylate to form L-pipecolate and L-proline, respectively [5].
• Interestingly, optimal functionality of MmGroEL/GroES and its ability to encapsulate larger proteins, such as malate dehydrogenase, requires the presence of ammonium sulfate in vitro [6].
• Structural analyses of a malate dehydrogenase with a variable active site [7].
• Malate dehydrogenase specifically oxidizes malate to oxaloacetate [7].

Chemical compound and disease context of mdh

• The malate dehydrogenase gene of Escherichia coli, which is susceptible to catabolite and anaerobic repression, has been cloned using plasmic pLC32-38 of Clarke and Carbon (1976) [8].
• Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution [9].
• The nucleotide sequence of a 1.1 kb XhoI-HindIII fragment downstream of the malate dehydrogenase (mdh) gene of Thermus flavus revealed the presence of an ORF and an incomplete ORF lacking its NH2-terminal portion, in the opposite orientation to that of the mdh gene [10].
• After fusion of six histidine codons to the 3'-end of the mdh gene and expression in Escherichia coli M15, active MDH was isolated using HisTrap purification [11].
• Kinetic studies and chemical modification studies using diethylpyrocarbonate and iodoacetate were performed on malate dehydrogenase isolated from Escherichia coli [12].

Biological context of mdh

• Measurements were made of cell viability, glyceraldehyde-3-phosphate dehydrogenase, malate dehydrogenase, lactate dehydrogenase, glutathione disulfide reductase, nonprotein sulfhydryl and total sulfhydryl compounds [13].
• The relative positions of argR (encoding arginine repressor) and mdh on the chromosome of S. typhimurium were determined from analysis of the nt sequence [14].
• A possible CRP binding site in the promotor region of the mdh gene provides evidence for a co-regulation with fumA gene, the structural gene of fumarase, which is also subject to catabolite repression [8].
• An oligodeoxynucleotide specific for a pentapeptide sequence corresponding to amino acid residues 32 through 36 of Escherichia coli malate dehydrogenase was chemically synthesized and used to identify the mdh gene on plasmid pLC32-38 from the Clarke-Carbon recombinant library [15].
• A proximal open reading frame, identified as the sucD gene, and the mdh gene may be parts of the same operon in T. aquaticus B [2].

Anatomical context of mdh

• The malate dehydrogenase isozyme MDH3 of Saccharomyces cerevisiae was found to be localized to peroxisomes by cellular fractionation and density gradient centrifugation [16].
• The MDHs purified to homogeneity from the high-expression clones were identical with the MDH isolated from T. aquaticus B cells with respect to all measured parameters [17].
• Adsorption of pre-purified human serum albumin (HSA) and malate dehydrogenase (MDH) displayed highest maximum binding capacities on HEC-coated dye-ligand-affinity membranes, ranging from (163 micrograms/cm2 for HSA to 316 micrograms/cm2 for MDH [18].

Associations of mdh with chemical compounds

• Effects on malate dehydrogenase, lactate dehydrogenase and glutathione disulfide reductase were negligible [13].
• The ternary complex of malate dehydrogenase has very few conformational differences from that of the pseudo binary complex of enzyme with bound citrate [19].
• Energy minimization of the structure with malate substituted for citrate in the active site shows that the nicotinamide moiety assumes the same position in the active site as the NAD in cytosolic malate dehydrogenase [19].
• The gene (mdh) coding for methanol dehydrogenase (MDH) of thermotolerant, methylotroph Bacillus methanolicus C1 has been cloned and sequenced [20].
• In the absence of ammonium sulfate, malate dehydrogenase fails to be encapsulated by GroES and rather cycles on and off the GroEL trans ring in a non-productive reaction [6].

Other interactions of mdh

• A 3 kb DNA fragment containing the gene (mdh) encoding malate dehydrogenase (MDH) from the thermophile Thermus aquaticus B was cloned in Escherichia coli and its nucleotide sequence determined [2].
• Multiplexed differential gene expression analysis is demonstrated on mdh and gyrB E. coli transcripts [21].

Analytical, diagnostic and therapeutic context of mdh

• The expression of the mdh gene, as measured by both Northern blotting and enzyme assays, was found to vary over a 20-fold range with different culture conditions [15].
• The structure of malate dehydrogenase from Escherichia coli complexed with the substrate analog, citrate and the cofactor NAD, has been determined by X-ray crystallography [19].
• Three enzymes (malate dehydrogenase, MD; NADH dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase, GPD) were tested for activity after treatment of E. coli with the test chemicals [22].
• By comparison of the gene sequences coding for malic acid dehydrogenase (mdh) of E. coli and non-E. coli strains, two oligonucleotides were designed and their possible use as E. coli-specific PCR primers was tested [23].
• Here we report the first direct visualization, by cryo-electron microscopy, of a non-native protein substrate (malate dehydrogenase) bound to the mobile, outer domains at one end of GroEL [24].

References