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

Mycobacterium vaccae strain JOB-5 cultured in the presence of propane contained an inducible secondary alcohol dehydrogenase. The enzyme was purified 198-fold using DEAE-cellulose, omega-aminopentyl agarose and NAD-agarose chromatography. The Mr of the enzyme was approximately 136000, with subunits of Mr 37000. The pH optimum for the reaction oxidizing propan-2-ol to propanone was 10-10.5 while the optimum for the reverse reaction was 7.5-8.5. The isoelectric point was 4.9. NAD but not NADP could serve as electron acceptor. The apparent Km values for propan-2-ol and NAD were 4.9 X 10(-5)M and 2.8 X 10(-4)M, respectively. The enzyme was inhibited by thiol reagents and metal chelators. It appears to play an essential role in the metabolism of propane by this bacterium.
J Gen Microbiol 1985 Nov
PMID:Purification and characterization of the secondary alcohol dehydrogenase from propane-utilizing Mycobacterium vaccae strain JOB-5. 391 61

Epithelial cells of the toad bladder were disaggregated with EDTA, trypsin, hyaluronidase, or collagenase and were then scraped free of the underlying connective tissue. In most experiments EDTA was complexed with a divalent cation before the tissue was scraped. Q(OO2), sucrose and inulin spaces, and electrolytes of the isolated cells were measured. Cells disaggregated by collagenase or hyaluronidase consumed O(2) at a rate of 4 microl hr(-1) dry wt(-1). Q(OO2) was increased 50% by ADH (100 U/liter) or by cyclic 3',5'-AMP (10 mM/liter). Na(+)-free Ringer's depressed the Q(OO2) by 40%. The Q(OO2) of cells prepared by trypsin treatment or by two EDTA methods was depressed by Na(+)-free Ringer's but was stimulated relatively little by ADH. Two other EDTA protocols produced cells that did not respond to Na(+) lack or ADH. The intracellular Na(+) and K(+) concentrations of collagenase-disaggregated cells were 32 and 117 mEq/kg cell H(2)O, respectively. Cation concentrations of hyaluronidase cells were similar, but cells that did not respond to ADH had higher intracellular Na(+) concentrations. Cells unresponsive to ADH and Na(+) lack had high sucrose spaces and low transcellular membrane gradients of Na(+), K(+), and Cl(-). The results suggest that trypsin and EDTA disaggregation damage the active Na(+) transport system of the isolated cell. Certain EDTA techniques may also produce a general increase in permeability. Collagenase and hyaluronidase cells appear to function normally.
J Gen Physiol 1968 Jun
PMID:Isolated epithelial cells of the toad bladder. Their preparation, oxygen consumption, and electrolyte content. 430 Jan 50

Mutations at the Adh1 locus in maize were selected from plants infected with barley stripe mosaic virus (BSMV). Pollen from the infected inbred line 1s2p, which is homozygous for Adh1-S (abbreviated S), Adh2-P, c and r was treated with allyl alcohol and applied to silks of a tester stock homozygous for Adh1-F, Adh2-N, C and R. From these pollinations 356 kernels arose on the F1 ears. Of these eight showed no activity of the S allele in scutellar samples while two exhibited low levels. Five of the putative mutant kernels germinated and two of these contained the contamination markers Adh2-P, c and r. The newly arisen mutations were designated S5446 and S5453. S5453 exhibited an abnormally low level of ADH activity in the F1 scutellum. In the F2 generation the mutant reverted at a high frequency with only about 5% of the S5453 alleles expressing low levels. DNA blotting and hybridization analyses showed no alterations in the restriction patterns of S5453 when compared to the progenitor S allele. S5446 which exhibited no ADH activity in the F1 scutellum is unstable in the pollen; reversion frequencies approaching 10(-2) were observed in samples from some plants. Restriction digestion patterns of DNA from this mutant revealed the presence of a 3.3 kb insertion at Adh. The insert does not appear to contain sequences homologous to the BSMV genome but rigorous analyses remain to be carried out. It is hypothesized that BSMV infection may mobilize endogenous but dormant transposable elements in maize.
Mol Gen Genet 1984
PMID:Mutations of the Adh1 gene in maize following infection with barley stripe mosaic virus. 609 61

Yeast translocatable, Ty, elements can cause constitutive synthesis of the glucose-repressible alcohol dehydrogenase (ADHII) when inserted upstream from the 5' end of the structural gene, ADR2. These insertion mutations, ADR3c, are unstable and give rise to secondary ADHII- mutations. The majority of such mutants, adr3, can be attributed to excision of the insertion sequence, leaving behind a single copy of the delta-sequence which occurs as a direct repeat at the ends of the Ty elements. A few adr3 mutants appear to be generated by DNA-rearrangements in the vicinity of the Ty insertion. The occurrence of recessive mutants, tye, which are unlinked to ADR2 indicates that the constitutive expression of ADR2 caused by the Ty insertions requires the function of trans-acting genes. These results support the idea that regulation of Ty-linked ADR2 is actively mediated by the insertion sequence and is probably not due to a mere disruption of the wild-type controlling site.
Mol Gen Genet 1981
PMID:Analysis of mutations affecting Ty-mediated gene expression in Saccharomyces cerevisiae. 626 30

It is shown that the unusual NAD(P)+-independent quinoprotein alcohol dehydrogenase, said previously to be responsible for oxidation of ethanol during growth of Acinetobacter calcoaceticus LMD 79.39, was in fact isolated from an unidentified organism which contained cytochrome c and which has now been lost. Several genuine strains of A. calcoaceticus do not contain cytochrome c nor do they contain a quinoprotein alcohol dehydrogenase. The enzyme responsible for ethanol oxidation in these bacteria is an inducible NAD+-linked alcohol dehydrogenase.
J Gen Microbiol 1983 Oct
PMID:The absence of quinoprotein alcohol dehydrogenase in Acinetobacter calcoaceticus. 631 94

We cloned sequences of the alk (alkane utilization) operon of Pseudomonas and characterized them physically and genetically. These sequences were used to construct a DNA restriction map of the alkBAC region. We physically mapped alk::Tn7 insertions and delta alkBA deletions, and we were able to show complementation or marker rescue of alk point mutations by cloned DNA sequences. Our results confirmed the existence of an operon containing structural loci encoding activities for membrane alkane hydroxylase component (alkB), soluble alkane hydroxylase component (alkA) and membrane alcohol dehydrogenase (alkC). Physical mapping of alkC::Tn7 insertions and complementation of alkC point mutations by cloned sequences from the alkBA region showed that we were previously mistaken in inferring the existence of a separate unlinked alkC cluster. Studies with an alkB-lacZ transcription fusion construct established that the operon is transcribed in the order alkBAC and is under positive regulation by alkR regulatory functions.
Mol Gen Genet 1984
PMID:Physical structure, genetic content and expression of the alkBAC operon. 639 91

We analyzed the reversion of strains carrying alk208, a mutation in the alkBAC (alkane utilization) region of the Pseudomonas CAM-OCT plasmid. Reversion of alk208 was stimulated 25 to 75-fold by small doses of UV-irradiation. All alkane hydroxylase-positive (AlkB+) revertants proved to be aliphatic alcohol dehydrogenase-positive (AlkC+) as well, whereas AlkC+ revertants could be either AlkB+ or AlkB-. Most of the AlkB- AlkC+ partial revertants produced AlkC- segregants at measurable frequencies. UV-irradiation substantially increased the rate of AlkC- segregation. Most segregants reverted to AlkB+ or AlkC+ at frequencies similar to the original alk208 strain. Dot blot hybridization analyses using cloned probes from various regions of CAM-OCT revealed that the partial revertants contained specific amplications of alk DNA. The endpoints of these amplifications mapped in at least two regions. AlkC- segregants had lost the DNA amplifications.
Mol Gen Genet 1984
PMID:Reversal by DNA amplifications of an unusual mutation blocking alkane and alcohol utilization in Pseudomonas putida. 659 34

Acinetobacter calcoaceticus grown on ethanol contains an NAD(P)+-independent alcohol dehydrogenase which resembles methanol dehydrogenase from methylotrophic bacteria in many respects. Likewise, the prosthetic group of this enzyme appears to be identical to that of methanol dehydrogenase, namely, pyrrolo quinoline quinone. The organism is unable to grow on methanol, which means that quinoprotein alcohol dehydrogenases are not restricted to methylotrophs. Arguments are presented for the idea that quinoprotein alcohol dehydrogenases exist in other alkane- or alcohol-grown bacteria. Although the enzyme from A. calcoaceticus can be best compared with that from Rhodopseudomonas acidophila in that both have very low affinities for methanol and are activated by aliphatic amines, the two enzymes are immunologically and electrophoretically unrelated. Furthermore, the A. calcoaceticus enzyme shows the broadest substrate specificity hitherto known for this type of enzyme in that it also oxidizes higher aldehydes. The extent of hydration of aldehydes cannot account for the aldehyde substrate specificity of these enzymes but the concept of a dual substrate specificity for alcohols and aldehydes can explain this very well. The different properties of the two enzymes compared with those of methanol dehydrogenases cannot be ascribed to the presence of iron as both enzymes contained a negligible amount of this metal.
J Gen Microbiol 1981 Feb
PMID:Quinoprotein alcohol dehydrogenase from a non-methylotroph, Acinetobacter calcoaceticus. 703 48

A strain of Escherichia coli with a mutation in the ana gene was shown to lack acetaldehyde dehydrogenase and alcohol dehydrogenase. The requirement of this strain for an external oxidant to grow anaerobically on glucose shows that the reduction of acetyl-CoA is the principal means of reoxidation of NADH produced during glycolysis in E. coli. Further mutants derived from the ana strain were shown to be affected in the enzymes involved in the fermentation of pyruvate (pyruvate formate-lyase, phosphotransacetylase, acetate kinase). A gene controlling acetate kinase (ackB) activity has been located at 39 min on the chromosomal map. Evidence is presented that anaerobic nitrite reduction with pyruvate involves at least the dehydrogenase subunit of the pyruvate dehydrogenase complex.
J Gen Microbiol 1981 May
PMID:Mutants of Escherichia coli K12 with defects in anaerobic pyruvate metabolism. 703 67

Mycobacterium tuberculosis var. bovis (BCG) grown on Sauton medium normally forms a pellicle; in the absence of added Zn2+, however, the pellicle sank during incubation and the yield was only about 20% of normal. The Zn2+-starved bacteria were morphologically similar to normal bacteria and were still acid-fast at 7 d as well as 14 d. The Zn2+-starved bacteria had slightly higher free lipid and phospholipid contents than normal; the content of hexoses was lower and proteins slightly lower. The deficient culture medium became opalescent and alkaline. Aspartate and ammonium ions accumulated. There was twice as much protein in deficient as in normal medium; moreover, a class of proteins precipitable at pH 4.5, which was hardly detectable in normal medium, was present in appreciable amounts of deficient medium. The content of aldehydes, measured with yeast alcohol dehydrogenase, was also doubled in deficient medium. Fractionation of acid-soluble aldehydes obtained from deficient medium after acid treatment of a bisulphite precipitate suggested the presence of several complex molecules bearing aldehyde groups. The need for Zn2+ in the medium may be explained by the presence in normal BCG of a Zn2+-requiring NADP-dependent alcohol dehydrogenase activity whose affinity for aldehydes is especially high.
J Gen Microbiol 1981 Jun
PMID:Effect of zinc deficiency on Mycobacterium tuberculosis var. bovis (BCG). 703 13


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