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:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intact pp60c-src, the cellular homologue of the transforming protein of Rous sarcoma virus, was purified from human platelets. The purified fractions also contained small amounts of a 54-kDa proteolytic degradation product of pp60c-src. We investigated some of the biochemical and kinetic properties of pp60c-src protein tyrosine kinase. Maximum kinase activity occurred at pH 6.5 and required a mixture of 2 mM Mn2+/Mg2+ as divalent cations. The enzyme most strongly phosphorylated casein, followed by enolase and alcohol dehydrogenase. The Km value for ATP was 4 microM for substrate phosphorylation and for autophosphorylation. Using casein, we determined a Vmax for substrate phosphorylation by pp60c-src in the range of 1.9-3.4 nmol.min-1.mg-1. Since the Vmax value for the purified 54-kDa fragment of pp60c-src was also included in this value, we conclude that proteolytic degradation of a 6-kDa fragment from the N-terminus of pp60c-src did not affect its kinase activity. Tryptic phosphopeptide analysis identified Tyr-416 as the major autophosphorylation site. Preincubation of purified pp60c-src with ATP increased the amount of autophosphorylation accompanied by an increase in Vmax, whereas the Km values were not altered. Our data directly demonstrate that autophosphorylation at Tyr-416 exerts, in contrast to phosphorylation at Tyr-527, a positive regulatory effect on the pp60c-src kinase activity.
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PMID:Characterization of purified pp60c-src protein tyrosine kinase from human platelets. 169 62

We show by deletion mutagenesis, followed by in vivo and in vitro analysis, that the binding of a protein factor to the upstream activation sequence (UAS) of the Saccharomyces cerevisiae glycolytic gene PYK, encoding pyruvate kinase, is required for efficient transcription of the corresponding coding region. In addition, gel electrophoretic mobility shift and DNase I protection studies, involving yeast gene products expressed in E. coli, suggest that this trans-acting DNA-binding protein is encoding by the RAP1 gene. The identification of RAP1 binding sites located within the UAS element of the yeast PYK, PGK (phosphoglycerate kinase) and ENO1 (enolase) genes, and in the 5'-upstream region of the ADHI (alcohol dehydrogenase) gene, suggests that a mechanism of coordinate gene expression involving several of the glycolytic genes may exist in yeast.
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PMID:The DNA-binding protein RAP1 is required for efficient transcriptional activation of the yeast PYK glycolytic gene. 212 35

Small cell lung cancers are neuroendocrine tumours and therefore produce a lot of peptide hormones (calcitonin, ACTH, ADH), as well as the neuropeptide chromogranin A, which are all useful tumour markers. Furthermore, the tumour-associated antigens CEA and TPA, as well as the enzymes neuron specific enolase (NSE) and creatine kinase BB are used as markers in small cell lung cancer. At present, NSE appears to be the best marker for small cell lung cancer; elevated serum NSE levels are found in 65 to 85% of the patients. The serum level of the tumour markers is related to the stage of the tumour. When tumour regression occurs following therapy, elevated pretreatment levels decrease to the normal range. If the marker level increases again, tumour progression is indicated and this can be an early and sensitive sign denoting recurrence. Metastases in the central nervous system can be detected early by marker determination in the cerebrospinal fluid. At present, CEA appears to be the most valuable tumour marker for non-small cell lung cancer, but TPA may also be a useful marker.
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PMID:[Tumor markers in bronchus cancer]. 254 31

N alpha-Acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl coenzyme A to the alpha-NH2 group of proteins and peptides, was isolated from Saccharomyces cerevisiae and demonstrated by protein sequence analysis to be NH2-terminally blocked. The enzyme was purified 4,600-fold to apparent homogeneity by successive purification steps using DEAE-Sepharose, hydroxylapatite, DE52 cellulose, and Affi-Gel blue. The Mr of the native enzyme was estimated to be 180,000 +/- 10,000 by gel filtration chromatography, and the Mr of each subunit was estimated to be 95,000 +/- 2,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has a pH optimum near 9.0, and its pI is 4.3 as determined by chromatofocusing on Mono-P. The enzyme catalyzed the transfer of an acetyl group to various synthetic peptides, including human adrenocorticotropic hormone (ACTH) (1-24) and its [Phe2] analogue, yeast alcohol dehydrogenase I (1-24), yeast alcohol dehydrogenase II (1-24), and human superoxide dismutase (1-24). These peptides contain either Ser or Ala as NH2-terminal residues which together with Met are the most commonly acetylated NH2-terminal residues (Persson, B., Flinta, C., von Heijne, G., and Jornvall, H. (1985) Eur. J. Biochem. 152, 523-527). Yeast enolase, containing a free NH2-terminal Ala residue, is known not to be N alpha-acetylated in vivo (Chin, C. C. Q., Brewer, J. M., and Wold, F. (1981) J. Biol. Chem. 256, 1377-1384), and enolase (1-24), a synthetic peptide mimicking the protein's NH2 terminus, was not acetylated in vitro by yeast acetyltransferase. The enzyme did not catalyze the N alpha-acetylation of other synthetic peptides including ACTH(11-24), ACTH(7-38), ACTH(18-39), human beta-endorphin, yeast superoxide dismutase (1-24). Each of these peptides has an NH2-terminal residue which is rarely acetylated in proteins (Lys, Phe, Arg, Tyr, Val, respectively). Among a series of divalent cations, Cu2+ and Zn2+ were demonstrated to be the most potent inhibitors. The enzyme was inactivated by chemical modification with diethyl pyrocarbonate and N-bromosuccinimide.
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PMID:Purification and characterization of an N alpha-acetyltransferase from Saccharomyces cerevisiae. 284 92

Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These results support suggestions that surface guanidino groups (arginyl groups) are an important factor in thermal stability of proteins.
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PMID:Arginyl residues and thermal stability in proteins. 353 44

In extracts of adult Angiostrongylus cantonensis, the activities of enzymes including glucokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, triosepho sphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglycerokinase, phosphoglyceromutase, enolase, pyruvate kinase, lactate dehydrogenase, pyruvate decarboxylase, alcohol dehydrogenase, glucose 6-phosphate dehydrogenase, glycerophosphate dehydrogenase and pyruvate dehydrogenase complex were demonstrated. The present of significant activity of glycerophosphate dehydrogenase and glucose 6-phosphate dehydrogenase may indicate the possibility of an operative of alpha-glycerophosphate and pentose phosphate pathway.
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PMID:Glycolytic enzymes in juvenile and adult Angiostrongylus cantonensis. 711 11

Autoimmune polyglandular syndrome type I (APS I) is associated with chronic mucocutaneous candidiasis. To characterize the antibody responses in this subgroup of Candida albicans infections, we screened a candidal cDNA expression library with patient sera and found four cDNA clones encoding the immunopositive proteins enolase, heat shock protein 90, pyruvate kinase, and alcohol dehydrogenase. The reactivity to these antigens was studied further by immunoprecipitation assays with in vitro-transcribed and -translated proteins. Analysis of sera from 44 APS I patients showed that the highest antibody reactivity was found with enolase (80% of patients reactive), but significant serological responses were also found with heat shock protein 90 (67%), pyruvate kinase (62.5%), and alcohol dehydrogenase (64%). Overall, 95.5% of patients had detectable antibodies to at least one of these proteins. The cDNAs of enolase and heat shock protein 90 were also expressed in Escherichia coli and studied by immunoblotting. Again, 84% of sera reacted with enolase, whereas 44% of sera reacted with heat shock protein 90. A good correlation between the two methods was found for both enolase (r = 0.86; n = 58; P < 0.001) and heat shock protein 90 (r = 0.71; n = 56; P < 0.001). Our results indicate that the four abundant candidal proteins are the major antigens and can be used as accurate markers of candidiasis in APS I patients. The immunoprecipitation assay described here is particularly useful for the rapid analysis of a large number of samples.
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PMID:Detection of candidal antigens in autoimmune polyglandular syndrome type I. 870 71

Fluoride released from methoxyflurane (MOF) during its hepatic and extrahepatic metabolism has been regarded as the major culprit responsible for MOF-induced nephrotoxicity. In the isolated, perfused rat kidney model, admixture of 1500 mumol/l fluoride to the perfusate resulted in tubular and glomerular damage with concomitant anuria. Fluoride administration in Fischer 344 rats in vivo elicited a renal diabetes insipidus-like syndrome that had also been observed in patients after MOF anaesthesia. The renal concentrating defect is most probably due to both dissipation of the corticomedullary osmolality gradient in the interstitium and failure of water reabsorption due to ADH refractoriness of the distal tubular cells. Hypothetically, the underlying mechanism may be a fluoride-induced inhibition of enzymes involved in intracellular energy production such as ATPase or enolase. The degree of nephrotoxicity correlates loosely with maximal serum fluoride levels, but can probably be modulated by further factors like intrarenal in situ formation of fluoride, urinary pH and flow, and especially, the presence of other nephrotoxins. This mitigates the importance of maximal fluoride serum levels, especially the 50 mumol threshold, as predictors of clinically relevant nephrotoxicity. To date, no nephrotoxic effects of sevoflurane could be demonstrated.
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PMID:[Nephrotoxicity and fluoride from the viewpoint of the nephrologist]. 877 2

The extent of genetic degeneration of the neo-Y chromosome of Drosophila americana americana has been investigated. Three loci, coding for the enzymes enolase, phosphoglycerate kinase and alcohol dehydrogenase, have been localized to chromosome 4 of D. a. americana, which forms the neo-Y and neo-X chromosomes. Crosses between D.a. americana and D. virilis or D. montana showed that the loci coding for these enzymes carry active alleles on the neo-Y chromosome in all wild-derived strains of americana that were tested. Intercrosses between a genetically marked stock of virilis and strains of americana were carried out, creating F3 males that were homozygous for sections of the neo-Y chromosome. The sex ratios in the F3 generation of the intercrosses showed that no lethal alleles have accumulated on any of the neo-Y chromosomes tested. There was evidence for more minor reductions in fitness, but this seems to be mainly caused by deleterious alleles that are specific to each strain. A similar picture was provided by examination of the segregation ratios of two marker genes among the F3 progeny. Overall, the data suggest that the neo-Y chromosome has undergone very little degeneration, certainly not to the extent of having lost the functions of vital genes. This is consistent with the recent origin of the neo-Y and neo-X chromosomes, and the slow rates at which the forces that cause Y chromosome degeneration are likely to work.
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PMID:Lack of degeneration of loci on the neo-Y chromosome of Drosophila americana americana. 909 52

In the present study we have analyzed protein oxidation on Escherichia coli when these cells were submitted to different stress conditions such as hydrogen peroxide, superoxide-generating compounds, and iron overloading. Carbonyl groups on oxidized cell proteins were examined by Western blot immunoassay. When anaerobically grown E. coli cells were exposed to hydrogen peroxide stress, alcohol dehydrogenase E, elongation factor G, the heat shock protein DNA K, oligopeptide-binding protein A, enolase, and the outer membrane protein A were identified as the major protein targets. A similar immunostained band pattern was found when cells were shifted from anaerobic to aerobic conditions in the presence of different concentrations of iron; it is relevant to note that oxidation of outer membrane protein C, not observed in peroxide stress conditions, was clearly detected as the concentration of iron was increased in the culture media. The hydrogen peroxide stress performed under aerobic conditions affected the beta-subunit of F0F1-ATPase; the rest of the oxidized protein pattern was very similar to that found for anaerobic conditions, with the exception of alcohol dehydrogenase E, a protein not synthesized aerobically. Cells submitted to superoxide stress using menadione showed a more specific pattern in which elongation factor G and the beta-subunit of F0F1-ATPase were affected significantly. When paraquat was used, although the degree of oxidative damage was lower, the same two modified proteins were detected, and DNA K was also clearly damaged. Cell viability was affected to different extents depending on the type of stress exerted. The results described in this paper provide data about the in vivo effects of oxidative stress on protein oxidation and give insights into understanding how such modifications can affect cellular functions.
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PMID:Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. 944 17


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