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)

Creatine kinase (CK) was used as a marker molecule to examine the side effect of damage to tissues by phenylbutazone (PB), an effective drug to treat rheumatic and arthritic diseases, with horseradish peroxidase and hydrogen peroxide (HRP-H(2)O2). PB inactivated CK during its interaction with HRP-H(2) O(2), and inactivated CK in rat heart homogenate. PB carbon-centered radicals were formed during the interaction of PB with HRP-H(2)O2. The CK efficiently reduced electron spin resonance signals of the PB carbon-centered radicals. The spin trap agent 2-methyl-2-nitrosopropane strongly prevented CK inactivation. These results show that CK was inactivated through interaction with PB carbon-centered radicals. Sulfhydryl groups and tryptophan residues in CK were lost during the interaction of PB with HRP-H(2)O2, suggesting that cysteine and tryptophan residues are oxidized by PB carbon-centered radicals. Other enzymes, including alcohol dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, but not lactate dehydrogenase, were also inactivated. Sulfhydryl enzymes seem to be sensitive to attack by PB carbon-centered radicals. Inhibition of SH enzymes may explain some of the deleterious effects induced by PB.
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PMID:Phenylbutazone radicals inactivate creatine kinase. 1126 93

This report enquires on the potentiality of Trp phosphorescence for probing the conformational state of proteins deposited on solid dry films. Thin, amorphous protein films were fabricated with Apoazurin, alcohol dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glutamate dehydrogenase the protein being incorporated into a DEAE-dextran matrix and deposited on quartz slides. The results, obtained with appositely constructed instrumentation, demonstrate that thanks to the low background radiation associated with long-lived, delayed emission phosphorescence can be readily detected down to single protein layer matrices and that both spectrum and lifetime are important indicators of the integrity of the protein globular fold. In fact, denaturation of the proteins by guanidinium hydrochloride or heat treatment points out that disruption of the native fold leads to a red shift and broadening of the spectrum with loss of vibronic structure, accompanied to considerably shorter-lived and more heterogeneous decay kinetics. It is also shown that the sensitivity of the phosphorescence lifetime towards the detection of altered, looser conformations of the polypeptide are remarkably enhanced on partial hydration of the sample.
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PMID:Tryptophan phosphorescence as a monitor of protein conformation in molecular films. 1141 43

The effects of a highly toxic coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl (PenCB), on triose phosphate metabolizing enzymes were studied. Male Wistar rats received 25 mg/kg PenCB, i.p. At this dose the compound provokes a wasting syndrome. The activity of triose phosphate metabolizing enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase, glycerokinase, transaldolase and transketolase were significantly reduced by PenCB treatment to 50%, 60%, 50%, 70% and 40% of free-fed controls, respectively. An inhibition study with pyrazol, a specific inhibitor of alcohol dehydrogenase (ADH), showed that ADH makes about a 30% contribution to the formation of glycerol-3-phosphate from glyceraldehyde-3-phosphate. Our current study revealed that PenCB suppresses ADH at the protein expression level. The reduced formation of glycerol-3-phosphate from glyceraldehyde dehydrogenase by PenCB could be due to the suppression of ADH. The triose phosphate content in the liver cytosol of PenCB-treated rats was significantly lower than in free-fed controls. The suppression of triose phosphate metabolism could be a cause of the wasting syndrome provoked by highly toxic coplanar PCB.
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PMID:Effects of a highly toxic coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl on intermediary metabolism: reduced triose phosphate content in rat liver cytosol. 1145 17

Two different strains of mice with different susceptibilities to systemic candidiasis (BALB/c and CBA/H) were infected with Candida albicans SC5314. Immune sera were obtained on different days post-infection and assayed against two-dimensional polyacrylamide gel electrophoresis separation of cytoplasmic extracts obtained from protoplasts. More than 31 immunoreactive proteins were detected. Some of them were identified and found to correspond to (i) glycolytic enzymes, such as fructose biphosphate aldolase, triose phosphate isomerase (TPIS), glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase (PGK), enolase (ENO1) and pyruvate kinase, (ii) other metabolic enzymes, such as methionine synthase (METE), inosine-5'-monophosphate dehydrogenase (IMH3), alcohol dehydrogenase and aconitate hydratase and (iii) heat shock proteins: HS71 (or Ssa1p) and HS75 (or Ssb1p), both from the HSP70 family. This work reports for the first time antigenic properties for IMH3 and TPIS. Different profiles of antibody expression, depending on the mouse strain and the course of infection, were observed. ENO1 was the most immunogenic protein in infected BALB/c mice (the most resistant strain). On the other hand, sera from CBA/H mice (a more susceptible strain) showed a strong increase in reactivity along the infection against METE, HS75 and PGK. Many of these immunoreactive proteins have also been detected using sera from human patients with systemic candidiasis, thus indicating the usefulness of the murine model for studying the antibody response in systemic candidiasis. In this work we demonstrate that the combination of two-dimensional electrophoresis with immunoblotting using murine immune sera can be an important tool for the identification of C. albicans antigens and for monitoring the evolution of the disease.
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PMID:Analysis of the serologic response to systemic Candida albicans infection in a murine model. 1168 Dec 8

Growth and starvation of baker's yeast was monitored by on-line microcalorimetry and cells originating from four different physiological states were stored at low temperature (4 degrees C) for up to 26 days. The different physiological states were designated F (respiro-Fermentative phase of growth), R (initial Respiratory phase of growth), -N (non-growing state because of Nitrogen depletion), and -NC (non-growing state because of both Nitrogen and Carbon depletion). The cells were tested before and after cold storage for their fermentative capacity, and characterised by 2D gel analysis (and subsequent quantitative silver staining and image analysis with software PDQUEST) for their levels of six enzymes of the glycolytic pathway (hexokinase 2 (Hxk2p), fructose bisphosphate aldolase (Fba1p), glyceraldehyde-3-phosphate dehydrogenase (Tdh3p), enolase A (Enolp), enolase B (Eno2p), and triose phosphate isomerase (Tpi1p)) and two enzymes of the fermentative branch (pyruvate decarboxylase (Pdc1p) and alcohol dehydrogenase (Adh1p)). The enzymes Hxk2p, Tdh3p, Eno2p, Pdc1p and Adh1p were down-regulated by 25-80% during the transition between the F and R states. During the transition to non-growing states (-N and -NC states), the levels of Hxk2p, Tdh3p and Eno2p were further reduced. However, after cold storage, the glycolytic and fermentative enzymes of the different physiological states were expressed to the same extent. In contrast, the fermentative capacity differed between the states; the R-state cells were superior compared to cells from the other states tested and preserved more than 50% of their initial fermentative capacity (6 mmol ethanol per gram dry weight and hour). Our data therefore clearly demonstrate that persistence of fermentative capacity during total starvation at low temperature after as long as 1 month is strongly dependent on the physiological state from which the cells originate. However, the level of expression of the glycolytic enzymes could not explain the difference in fermentative capacity of the different physiological states after cold storage.
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PMID:Fermentative capacity after cold storage of baker's yeast is dependent on the initial physiological state but not correlated to the levels of glycolytic enzymes. 1178 28

In cattle, administration of retinol at the time of superovulation has been indirectly associated with enhanced developmental potential of the embryo. Vitamin A and its metabolites influence several developmental processes by interacting with 2 different types of nuclear receptors, retinoic acid receptors and retinoid X receptors (RXRs). Given the limited information available concerning the RXR-mediated retinoid signaling system, particularly in species other than rodents, this study was performed to gain insight into the potential role of retinoid signaling during preattachment embryo development in the cow. Bovine embryos were produced in vitro from oocytes harvested from abattoir ovaries and frozen in liquid nitrogen at the oocyte, 2-, 4-, 8-, and 16- to 20-cell, morula, blastocyst, and hatched blastocyst stages. Reverse transcription polymerase chain reaction (PCR) and whole mount in situ hybridization were utilized to investigate mRNA expression for RXR alpha, RXR beta, RXR gamma, alcohol dehydrogenase I (ADH-I), retinaldehyde dehydrogenase 2 (RALDH2), peroxisome proliferator activated receptor gamma (PPAR gamma), and glyceraldehyde-3-phosphate dehydrogenase. Transcripts for RXR alpha, RXR beta, RALDH2, and PPAR gamma were detected in all stages beginning from the oocyte through to the hatched blastocyst. Whole mount in situ hybridization performed using digoxigenin-labeled antisense probes detected all 4 transcripts in both the inner cell mass and the trophectoderm of hatched blastocysts. PCR products obtained for ADH-I exhibited very low homology to known human and mouse sequences. Immunohistochemistry was performed using polyclonal anti-rabbit antibodies against RXR beta and PPAR gamma to investigate whether these embryonic mRNAs were translated to the mature protein. Strong immunostaining was observed for both RXR beta and PPAR gamma in the trophectoderm and inner cell mass cells of intact and hatched blastocysts. Messenger RNA was not detected at any stage for RXR gamma. Expression of mRNA for RXR alpha, RXR beta, RALDH2, and PPAR gamma suggests that the early embryo may be competent to synthesize retinoic acid and regulate gene expression during preattachment development in vitro.
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PMID:Expression patterns of retinoid X receptors, retinaldehyde dehydrogenase, and peroxisome proliferator activated receptor gamma in bovine preattachment embryos. 1187 76

Creatine kinase (CK) was used as a marker molecule to examine the side effects of damage to tissues by mefenamic acid, an effective drug to treat rheumatic and arthritic diseases, with horseradish peroxidase and hydrogen peroxide (HRP-H(2)O(2)). Mefenamic acid inactivated CK during its interaction with HRP-H(2)O(2). Also, diphenylamine and flufenamic acid caused a loss of CK activity, indicating the imino group, not substituent groups, in the phenyl rings have a crucial role in CK inactivation. Rapid change in mefenamic acid spectra was detected, suggesting that mefenamic acid is efficiently oxidized by HRP-H(2)O(2). Peroxidases oxidize xenobiotics to free radicals by a one-electron transfer. However, direct detection of mefenamic acid radicals by electron spin resonance (ESR) was unsuccessful. Reduced glutathione and 5,5-dimethyl-1-pyrroline-1-oxide (DMPO) in the reaction mixture containing mefenamic acid with HRP-H(2)O(2) produced ESR signals consistent with a DMPO-glutathionyl radical adduct. These results suggest that inactivation of CK is probably caused through formation of mefenamic acid radicals. Sulfhydryl groups and tryptophan residues of CK were diminished by mefenamic acid with HRP-H(2)O(2). Other SH enzymes, including alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase, were very sensitive to mefenamic acid with HRP-H(2)O(2). Inactivation of SH enzymes may explain some deleterious actions of mefenamic acid.
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PMID:Inactivation of creatine kinase during the interaction of mefenamic acid with horseradish peroxidase and hydrogen peroxide: participation by the mefenamic acid radical. 1259 89

Neurospora crassa, a filamentous fungus, naturally produces the carotenoids lycopene and neurosporaxanthin. To increase the carbon flux through the carotenoid biosynthetic pathway, the 1658-bp region of the HMG1 gene encoding the catalytic domain (cHMG1) of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase of Saccharomyces cerevisiae was expressed in N. crassa under control of the strong, constitutive glyceraldehyde-3-phosphate dehydrogenase (GPD) promoter and the inducible alcohol dehydrogenase (alcA) promoter. Overexpressing cHMG1 under control of the GPD promoter increased lycopene and neurosporaxanthin production 6- and 1.5-fold, respectively, relative to the wild-type strain. Over-expression of cHMG1 under control of the alcA promoter increased production of lycopene and neurosporaxanthin 3- and 2-fold, respectively.
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PMID:Amplification of HMG-CoA reductase production enhances carotenoid accumulation in Neurospora crassa. 1261 89

Several microbial pathogens augment their invasive potential by binding and activating human plasminogen to generate the proteolytic enzyme plasmin. Yeast cells and cell wall proteins (CWP) of the human pathogenic fungus Candida albicans bound plasminogen with a K(d) of 70 +/- 11 nM and 112 +/- 20 nM respectively. Bound plasminogen could be activated to plasmin by mammalian plasminogen activators; no C. albicans plasminogen activator was detected. Binding of plasminogen to CWP and whole cells was inhibited by epsilon ACA, indicating that binding was predominantly to lysine residues. Candida albicans mutant strains defective in protein glycosylation did not show altered plasminogen binding, suggesting that binding was not mediated via a surface lectin. Binding was sensitive to digestion by basic carboxypeptidase, implicating C-terminal lysine residues in binding. Proteomic analysis identified eight major plasminogen-binding proteins in isolated CWP. Five of these (phosphoglycerate mutase, alcohol dehydrogenase, thioredoxin peroxidase, catalase, transcription elongation factor) had C-terminal lysine residues and three (glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and fructose bisphosphate aldolase) did not. Activation of plasminogen could potentially increase the capacity of this pathogenic fungus for tissue invasion and necrosis. Although surface-bound plasmin(ogen) degraded fibrin, no direct evidence for a role in invasion of endothelial matrix or in penetration and damage of endothelial cells was found.
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PMID:Candida albicans binds human plasminogen: identification of eight plasminogen-binding proteins. 1262 18

The irreversible oxidation of cysteine residues can be prevented by protein S-thiolation, a process by which protein SH groups form mixed disulphides with low-molecular-mass thiols such as glutathione. We report here the target proteins which are modified in yeast cells in response to H(2)O(2). In particular, a range of glycolytic and related enzymes (Tdh3, Eno2, Adh1, Tpi1, Ald6 and Fba1), as well as translation factors (Tef2, Tef5, Nip1 and Rps5) are identified. The oxidative stress conditions used to induce S-thiolation are shown to inhibit GAPDH (glyceraldehyde-3-phosphate dehydrogenase), enolase and alcohol dehydrogenase activities, whereas they have no effect on aldolase, triose phosphate isomerase or aldehyde dehydrogenase activities. The inhibition of GAPDH, enolase and alcohol dehydrogenase is readily reversible once the oxidant is removed. In addition, we show that peroxide stress has little or no effect on glucose-6-phosphate dehydrogenase or 6-phosphogluconate dehydrogenase, the enzymes that catalyse NADPH production via the pentose phosphate pathway. Thus the inhibition of glycolytic flux is proposed to result in glucose equivalents entering the pentose phosphate pathway for the generation of NADPH. Radiolabelling is used to confirm that peroxide stress results in a rapid and reversible inhibition of protein synthesis. Furthermore, we show that glycolytic enzyme activities and protein synthesis are irreversibly inhibited in a mutant that lacks glutathione, and hence cannot modify proteins by S-thiolation. In summary, protein S-thiolation appears to serve an adaptive function during exposure to an oxidative stress by reprogramming metabolism and protecting protein synthesis against irreversible oxidation.
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PMID:Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. 1275 85


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