Search results for "alcohol dehydrogenase"

showing 10 items of 35 documents

Heavy enzymes and the rational redesign of protein catalysts

2019

Abstract An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Comparison between isotopically labelled “heavy” dihydrofolate reductases and their natural‐abundance counterparts has suggested that the coupling of protein motions to the chemistry of the catalysed reaction is minimised in the case of hydride transfer. In alcohol dehydrogenases, unnatural, bulky substrates that induce additional electrostatic rearrangements of the active site enhance coupled motions. This finding could provide a new route to engineering enzymes with altered substrate specificity, because amino acid residues responsible for dynamic coupling with a given substrate present…

010402 general chemistryProtein Engineering01 natural sciencesBiochemistryCatalysisEnzyme catalysisisotope effectsCatalytic DomainDihydrofolate reductaseMolecular BiologyAlcohol dehydrogenasechemistry.chemical_classificationalcohol dehydrogenasesCarbon Isotopesdihydrofolate reductasesbiologyBacteriaNitrogen Isotopes010405 organic chemistryConceptOrganic ChemistryAlcohol DehydrogenaseActive siteSubstrate (chemistry)Protein engineeringDeuteriumCombinatorial chemistrymolecular dynamics0104 chemical sciencesKineticsTetrahydrofolate Dehydrogenaseenzyme engineeringEnzymechemistrybiology.proteinBiocatalysisMolecular MedicineConcepts
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2017

Previous studies reported that the use of Metschnikowia pulcherrima in sequential culture fermentation with Saccharomyces cerevisiae mainly induced a reduction of volatile acidity in wine. The impact of the presence of this yeast on the metabolic pathway involved in pyruvate dehydrogenase (PDH) bypass and glycerol production in S. cerevisiae has never been investigated. In this work, we compared acetic acid and glycerol production kinetics between pure S. cerevisiae culture and its sequential culture with M. pulcherrima during alcoholic fermentation. In parallel, the expression levels of the principal genes involved in PDH bypass and glyceropyruvic fermentation in S. cerevisiae were investi…

0301 basic medicineMicrobiology (medical)Fermentation in winemaking030106 microbiologyfood and beveragesBiologyEthanol fermentationbiology.organism_classificationPyruvate dehydrogenase complexMicrobiologyYeast03 medical and health sciencesBiochemistrybiology.proteinFermentationPyruvate decarboxylaseMetschnikowia pulcherrimaAlcohol dehydrogenaseFrontiers in Microbiology
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2018

The origin of substrate preference in promiscuous enzymes was investigated by enzyme isotope labelling of the alcohol dehydrogenase from Geobacillus stearothermophilus (BsADH). At physiological temperature, protein dynamic coupling to the reaction coordinate was insignificant. However, the extent of dynamic coupling was highly substrate-dependent at lower temperatures. For benzyl alcohol, an enzyme isotope effect larger than unity was observed, whereas the enzyme isotope effect was close to unity for isopropanol. Frequency motion analysis on the transition states revealed that residues surrounding the active site undergo substantial displacement during catalysis for sterically bulky alcohol…

0301 basic medicinebiologyChemistryStereochemistrySubstrate (chemistry)Active siteGeneral Chemistry010402 general chemistry01 natural sciencesCatalysisTransition state0104 chemical sciencesEnzyme catalysisReaction coordinate03 medical and health scienceschemistry.chemical_compound030104 developmental biologyBenzyl alcoholKinetic isotope effectbiology.proteinAlcohol dehydrogenaseAngewandte Chemie International Edition
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Genetic contribution to alcohol dependence: Investigation of a heterogeneous german sample of individuals with alcohol dependence, chronic alcoholic …

2017

The present study investigated the genetic contribution to alcohol dependence (AD) using genome-wide association data from three German samples. These comprised patients with: (i) AD; (ii) chronic alcoholic pancreatitis (ACP); and (iii) alcohol-related liver cirrhosis (ALC). Single marker, gene-based, and pathway analyses were conducted. A significant association was detected for the ADH1B locus in a gene-based approach (puncorrected = 1.2 × 10-6; pcorrected = 0.020). This was driven by the AD subsample. No association with ADH1B was found in the combined ACP + ALC sample. On first inspection, this seems surprising, since ADH1B is a robustly replicated risk gene for AD and may therefore be …

0301 basic medicinemedicine.medical_specialtyCirrhosislcsh:QH426-470alcohol dependenceMedizinGenome-wide association studyLocus (genetics)610 Medicine & healthGastroenterologyArticle03 medical and health sciencesLiver diseaseInternal medicineGeneticsMedicine610 Medicine &amp; healthAllele frequencyGenetics (clinical)genome-wide association studybusiness.industryAlcohol dependencealcohol dehydrogenaseADH1Bchronic alcoholic pancreatitisalcohol dependence; chronic alcoholic pancreatitis; alcoholic liver cirrhosis; genome-wide association study; alcohol dehydrogenase; <i>ADH1B</i>; <i>ADH1C</i>medicine.diseaseADH1CADH1Blcsh:Genetics030104 developmental biologyPancreatitisalcoholic liver cirrhosisbusiness
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Diacetyl and acetoin production from the co-metabolism of citrate and xylose by Leuconostoc mesenteroides subsp. mesenteroides.

1997

The co-metabolism of citrate plus xylose by Leuconostoc mesenteroides subsp. mesenteroides results in a growth stimulation, an increase in D-lactate and acetate production and repression of ethanol production. This correlated well with the levels of key enzymes involved. A partial repression of alcohol dehydrogenase and a marked stimulation of acetate kinase were observed. High citrate bioconversion yields in diacetyl plus acetoin were obtained at pH 5.2 in batch (11.5%) or in chemostat (up to 17.4%) culture. In contrast, no diacetyl or acetoin was detected in citrate plus glucose fermentation.

Acetate kinaseXylosebiologyAcetoinAcetoinGeneral MedicineDiacetylXylosebiology.organism_classificationNADApplied Microbiology and BiotechnologyDiacetylCitric Acidchemistry.chemical_compoundchemistryBiochemistryXylose metabolismLeuconostoc mesenteroidesbiology.proteinFermentationLeuconostocBiotechnologyAlcohol dehydrogenaseApplied microbiology and biotechnology
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Genome-wide Association Study of Alcohol Dependence

2009

Context Alcohol dependence is a serious and common public health problem. It is well established that genetic factors play a major role in the development of this disorder. Identification of genes that contribute to alcohol dependence will improve our understanding of the mechanisms that underlie this disorder. Objective To identify susceptibility genes for alcohol dependence through a genome-wide association study (GWAS) and a follow-up study in a population of German male inpatients with an early age at onset. Design The GWAS tested 524 396 single-nucleotide polymorphisms (SNPs). All SNPs with P −4 were subjected to the follow-up study. In addition, nominally significant SNPs from genes t…

AdultGenetic MarkersMaleGenotypeGenetic LinkagePopulationContext (language use)Single-nucleotide polymorphismGenome-wide association studyBiologyPolymorphism Single NucleotideGenetic determinismArticleAlcohol Withdrawal DeliriumYoung AdultArts and Humanities (miscellaneous)Genetic linkageAnimalsHumansAlleleAge of OnseteducationAllelesGeneticseducation.field_of_studyGene Expression ProfilingAlcohol dependenceAlcohol DehydrogenasePutamenRats Inbred StrainsAmygdalaCadherinsRatsHospitalizationPsychiatry and Mental healthAlcoholismPhenotypeGene Expression RegulationCase-Control StudiesChromosomes Human Pair 2Caudate NucleusLod ScoreFollow-Up StudiesGenome-Wide Association Study
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Spectrum of mutations and phenotypic expression in patients with autosomal dominant hypercholesterolemia identified in Italy.

2013

Abstract Objective To determine the spectrum of gene mutations and the genotype–phenotype correlations in patients with Autosomal Dominant Hypercholesterolemia (ADH) identified in Italy. Methods The resequencing of LDLR , PCSK9 genes and a selected region of APOB gene were conducted in 1018 index subjects clinically heterozygous ADH and in 52 patients clinically homozygous ADH. The analysis was also extended to 1008 family members of mutation positive subjects. Results Mutations were detected in 832 individuals: 97.4% with LDLR mutations, 2.2% with APOB mutations and 0.36% with PCSK9 mutations. Among the patients with homozygous ADH, 51 were carriers of LDLR mutations and one was an LDLR / …

Adultmedicine.medical_specialtyHeterozygoteSettore MED/09 - Medicina InternaApolipoprotein BCoronary DiseaseBiologyGene mutationmedicine.disease_causeHyperlipoproteinemia Type IITendonschemistry.chemical_compoundReference ValuesInternal medicinemedicineXanthomatosisHumansGeneAllelesGenetic Association StudiesAgedGeneticsMutationCholesterolPCSK9Cholesterol HDLSerine EndopeptidasesSmokingAlcohol Dehydrogenasenutritional and metabolic diseasesCholesterol LDLMiddle AgedEndocrinologyPhenotypechemistryItalyLDL receptorMutationbiology.proteinAutosomal dominanthypercholesterolemia LDL receptor Apolipoprotein B PCSK9 Mutationslipids (amino acids peptides and proteins)Allelic heterogeneityFemaleProprotein ConvertasesProprotein Convertase 9Cardiology and Cardiovascular MedicineAtherosclerosis
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Relationships between oxygen concentration and patterns of energy metabolism in the rotifer Brachionus plicatilis

1992

Abstract 1. 1. Activities of 10 enzymes and accumulation of two metabolites under experimental hypoxia were investigated in the rotifer Brachionus plicatilis . 2. 2. Pyruvate kinase (PK), lactate dehydrogenase (LDH), malic enzyme (ME), phosphoenolpyruvate carboxykinase (PEPCK), malate dehydrogenase (MDH) and fumarase (FUM) activities showed great increase at low oxygen levels. Alcohol dehydrogenase (ADH) activity was not detected. 3. 3. Alanine concentration showed an increase with low oxygen concentrations, while alanine aminotransferase (GTP) showed a slight activity increase with oxygen levels. The high alanine concentration was interpreted as enhanced proteolysis. 4. 4. Our results show…

AlaninebiologyPhysiologyMalic enzymeGeneral MedicineBrachionusbiology.organism_classificationBiochemistryMalate dehydrogenasechemistry.chemical_compoundBiochemistrychemistryLactate dehydrogenasebiology.proteinLimiting oxygen concentrationMolecular BiologyPyruvate kinaseAlcohol dehydrogenaseComparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Potential of microorganisms to decrease the "beany" off-flavor

2022

Alcohol dehydrogenaseVolatile compoundsMicroorganismsAldehyde dehydrogenase[SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology"beany" off-flavor
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Glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2). New evidence for differential expres…

2011

Epidemiological and experimental studies support the involvement of lipid peroxidation (LPO) in retinal diseases. In addition to other pathogenic mechanisms not fully understood, the possibility remains that peroxidic aldehydes, acting as cytotoxic chemicals, mediate in the progression of chronic ocular disorders.To test proper mechanisms involved in removing peroxidic aldehydes from the retina, in an attempt to understand long-lasting changes induced by LPO, the oxidative and antioxidant enzymatic activities, as well as the retinal distribution and activity of glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2), were studied and c…

Aldehyde dehydrogenaseBiologymedicine.disease_causeBiochemistryRetinaLipid peroxidationMitochondrial Proteinschemistry.chemical_compoundRetinal DiseasesmedicineAnimalsRats WistarFormaldehyde dehydrogenaseALDH2Alcohol dehydrogenaseAldehyde Dehydrogenase MitochondrialAlcohol DehydrogenaseRetinalGeneral MedicineGlutathioneAldehyde DehydrogenaseMolecular biologyGlutathioneImmunohistochemistryRatsOxidative StresschemistryBiochemistrybiology.proteinFemaleLipid PeroxidationOxidative stressFree radical research
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