Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Study of AMPc phosphodiesterase shows presence of JH in diapausing chrysalids and antogonistic action of FH and pterines. Study of farnesoldeshydrogenase and farnesal deshydrogenase in Dm shows that FH4 and pterines inhibite FDH, active ADH. Conclusion is JH in diapause chrysalides is active factor with FH4 provoking genesis of pigmentary mutation, cellular proliferation or growth deficiencies. Comparison with JH+FH4+ teromes incubated in Bar (Muller 5) mutants of Dm in place of diapausing chrysalids reproduce larval deficiences, mosaics and mutations observed in precedent experiments.
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PMID:[Juvenile hormone in diapausing Pieris brassicae and mutations. Tetrahydrofolic acid and pterins incubated in chrysalids, provoking ontogenic and mutagenic genetic information alterations in Drosophila melanogaster]. 17 4

Of the five human alcohol dehydrogenase (ADH) genes located in the region q21-25 of chromosome 4, genetic markers have been reported previously only for class I enzymes, ADH1-3. Here, new restriction fragment length polymorphisms (RFLPs) are described for the genes of two other classes, ADH4 (pi) and ADH5 (chi or formaldehyde dehydrogenase, FDH). The frequencies and modes of inheritance of these RFLPs were determined with DNA both from unrelated individuals and from families. A polymorphic PstI site is assigned to the fourth intron of the ADH4 gene. Pairwise linkage disequilibrium calculations for these new RFLPs and already known RFLPs at the ADH2 and ADH3 loci establish strong linkage disequilibria between polymorphic MspI and BstXI sites in the ADH5 gene as well as between XbaI and MspI sites in the ADH3 gene. Furthermore, linkage disequilibria were detected between RFLPs of the ADH2 and ADH3 genes as well as between those of the ADH4 and ADH5 genes. The latter disequilibrium implies a hitherto unknown physical proximity of two genes belonging to different ADH classes. The RFLPs were used to construct chromosomal haplotypes that include three ADH classes. Of the 16 possible haplotypes for four RFLP markers used here, 10 were experimentally detected. The potential application of the ADH RFLPs and haplotypes in linkage or association studies of inherited diseases such as familial "alcoholism" is discussed.
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PMID:Alcohol dehydrogenase genes: restriction fragment length polymorphisms for ADH4 (pi-ADH) and ADH5 (chi-ADH) and construction of haplotypes among different ADH classes. 136 87

Three different dehydrogenases able to oxidize formaldehyde were found in the Gram-positive methylotroph, Nocardia sp. 239: an NAD-dependent aldehyde dehydrogenase (NA-ADH), and NAD- and factor-dependent formaldehyde dehydrogenase (FD-FDH), and a dye-linked aldehyde dehydrogenase (DL-ADH). The ratio of the activities observed for the two NAD-linked enzymes varied with growth conditions: batch-wise grown cells had nearly the same activities for both enzymes; in fed batch-wise grown cells (methanol limitation) only FD-FDH was detected. The latter is clearly involved in formaldehyde oxidation, since the enzyme and the factor were found only in methanol-grown cells and the enzyme is specific for formaldehyde. In contrast, the two aldehyde dehydrogenases may have significance for aldehyde dissimilation in general, since both activities could also be demonstrated in ethanol-grown cells (but not in glucose-grown cells) and higher aldehydes are even better substrates than formaldehyde. NA-ADH was purified to homogeneity. The enzyme seems to be a homotetramer since it showed a relative molecular mass of 200,000 and the denaturated form of 55,000. Other characteristics are as follows: the enzyme showed substrate inhibition for the aldehydes tested; optimal activity was found at pH 9.2; the reverse reaction was not observed; the enzyme was specific for NAD; GSH, K+, or NH4+ addition did not stimulate formaldehyde oxidation; the order of NAD and substrate addition to the enzyme was not important; several compounds able to block SH groups were inhibitory. Comparison with NAD-linked aldehyde dehydrogenases from Gram-negative bacteria showed that the Nocardia enzyme is distinct from the enzyme of Pseudomonas putida (EC 1.2.1.46) and of Hyphomicrobium X.
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PMID:Different types of formaldehyde-oxidizing dehydrogenases in Nocardia species 239: purification and characterization of an NAD-dependent aldehyde dehydrogenase. 224 Nov 49

We developed and evaluated an assay for serum uric acid based on the uricase (EC 1.7.3.3)-catalase (EC 1.11.1.6)-formaldehyde dehydrogenase (FADH, EC 1.2.1.46) method coupled with formate dehydrogenase (formate:NAD oxidoreductase, FDH, EC 1.2.1.2). Formate dehydrogenase from Pseudomonas oxalaticus catalyzes the formation of NADH from formate produced by FADH. Owing to the NADH and formate oxidase activity of the FDH itself, the full reaction curve is not linear, but gradually decreases. The formation of NADH is not stoichiometric with formate removal, but is strictly proportional to it. To overcome this decrease of extinction, we added hydroxylamine hydrochloride to the FDH. The sensitivity of the full reaction in the presence of FDH was about 1.8 times that without FDH. Analysis with a Cobas Bio centrifugal analyzer revealed a linearity of up to 3.56 mmol/L. The uricase-catalase-alcohol dehydrogenase method correlated well with the uricase-peroxidase-chromogen method. Our method is more sensitive than other methods.
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PMID:A sensitive determination of uric acid in serum using uricase/catalase/formaldehyde dehydrogenase coupled with formate dehydrogenase. 807 73

A DNA fragment of 485 bp was specifically amplified by PCR with primers based on the N-terminal sequence of the purified formaldehyde dehydrogenase (EC 1.2.1.46) from Pseudomonas putida and on that of a cyanogen bromide-derived peptide. With this product as a probe, a gene coding for formaldehyde dehydrogenase (fdhA) in P. putida chromosomal DNA was cloned in Escherichia coli DH5 alpha. Sequencing analysis revealed that the fdhA gene contained 1,197-bp open reading frame, encoding a protein composed of 399 amino acid residues whose calculated molecular weight was 42,082. The transformant of E. coli DH5 alpha harboring the hybrid plasmid, pFDHK3DN71, showed about 50-fold-higher formaldehyde dehydrogenase activity than P. putida. The predicted amino acid sequence contained several features characteristic of the zinc-containing medium-chain alcohol dehydrogenase (ADH) family. Most of the glycine residues strictly conserved within the family, including a Gly-Xaa-Gly-Xaa-Xaa-Gly pattern in the coenzyme binding domain, were well conserved in this enzyme. Regions around both the catalytic and the structural zinc atoms were also conserved. Analyses of structural and enzymatic characteristics indicated that P. putida FDH belongs to the medium-chain ADH family, with mixed properties of mammalian class I and III ADHs.
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PMID:Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida. 816 97

Modification of class III alcohol dehydrogenase (chi chi-ADH) with phenylglyoxal eliminates fatty acid activation by pentanoate and octanoate and concomitantly increases specific activity toward ethanol and 3-methylcrotyl alcohol 2-3-fold. In contrast, chemical modification decreases activity toward S-(hydroxymethyl)glutathione (FDH activity) and 12-hydroxydodecanoic acid by increasing Km, pointing to a role for arginine in binding anionic substrates. Modification with [7-14C]phenylglyoxal indicates that only one arginine residue per subunit is modified. Sequence analysis of tryptic peptides indicates that Arg-115 is modified. Site-directed mutation of this residue to alanine eliminates both fatty acid activation and FDH activity, thus confirming the identity of the modified residue and its function. These results account in part for the unique specificity of chi chi-ADH relative to other human ADH isozymes.
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PMID:Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. 849 91

Electrophoretic spectra of GOT, GDH, DIA, MDH, SOD, FDH, ADH, ACP, IDH enzymes in the megagametophytes of seeds of 69 mountain pine (Pinus mugo Turra) trees from natural populations of the Ukrainian Carpathian mountains have been described. 19 loci products had efficient electrophoretic separation. The analysis of alleles segregation of the heterozygous trees on the whole confirms monogenic inheritance of the discovered variants.
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PMID:[Genetic diversity of isoenzymes in mountain pine (Pinus mugo Turra) in natural populations in the Ukrainian Carpathian mountains]. 1121 32

Genetic control of GOT, GDH, DIA, MDH, SOD, FDH, ADH, ACP, and LAP enzymes was studied in the seed megagametophytes of cembra pine (Pinus cembra L.) from the natural population of the Ukrainian Carpa-thian mountains. Efficient electrophoretic separation was obtained for 21 loci products. The analysis of allele segregation in heterozygous trees confirms monogenic inheritance of the revealed variants.
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PMID:[Genetic control of the isoenzymes in Cembra pine (Pinus cembra L.) in the Ukrainian Carpathian Mountains]. 1183 36

The genetic control of 9 enzymous systems in 46 trees of Pinus pityusa Stev. of two isolated Crimean populations was studied using electrophoretic separation of izsozymes in vertical plates of polyacrylamide gel. The detailed description of electrophoretic spectra of ADH, ACP, DIA, GOT, GDH, LAP, MDH, FDH, and SOD encoded by 20 loci is presented. The comparative analysis of the results published data on these allozymous loci in closely related pine species of genus Pinus L. was made.
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PMID:[Genetic control of allozymes of Pinus pityusa Stev. in natural Crimean populations]. 1201 92

[reaction: see text] An enzyme-compatible biphasic reaction media for the asymmetric biocatalytic reduction of ketones with in situ cofactor regeneration has been developed. In this biphasic reaction media, which is advantageous for reactions at higher substrate concentrations, both enzymes (alcohol dehydrogenase and FDH from Candida boidinii) remain stable. The reductions with poorly water-soluble ketones were carried out at substrate concentrations of 10-200 mM, and the optically active (S)-alcohols were formed with moderate to good conversions and with up to >99% ee.
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PMID:Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media. 1252 33


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