2015
Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology
Jackson BC, Thompson DC, Charkoftaki G, Vasiliou V. Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology. Expert Opinion On Drug Metabolism & Toxicology 2015, 11: 1839-1847. PMID: 26558415, PMCID: PMC4937717, DOI: 10.1517/17425255.2016.1108406.Peer-Reviewed Original ResearchConceptsAldehyde dehydrogenase gene familiesDehydrogenase gene familyDead enzymesGene familyActive enzymeProtein-protein interactionsTotal enzyme populationNon-enzymatic functionsALDH proteinsAvailability of substratesSubcellular spaceGene productsKey residuesProtein recordsCatalytic activityEnzyme populationPathophysiological functionsAllosteric modulationEnzymeBiological actionsProteinBiological activityComputational analysisALDHFamily
2013
ALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1
Vasiliou V, Sandoval M, Backos DS, Jackson BC, Chen Y, Reigan P, Lanaspa MA, Johnson RJ, Koppaka V, Thompson DC. ALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1. Chemico-Biological Interactions 2013, 202: 22-31. PMID: 23348497, PMCID: PMC3746320, DOI: 10.1016/j.cbi.2012.12.018.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsSingle nucleotide polymorphismsSuch protein-protein interactionsCoiled-coil domainImportant cysteine residuesMissense single nucleotide polymorphismMost mammalian speciesALDH domainHuman cell linesALDH16A1Cysteine residuesMammalian speciesProtein structureUnique memberKey enzymeEtiology of goutGenesNucleotide polymorphismsHPRT activityProteinAcid metabolismCell linesLong formIntriguing possibilityLower animals
2012
Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2
Jackson BC, Holmes RS, Backos DS, Reigan P, Thompson DC, Vasiliou V. Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2. Chemico-Biological Interactions 2012, 202: 11-21. PMID: 23247008, PMCID: PMC3687035, DOI: 10.1016/j.cbi.2012.11.022.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsAnuraComputer SimulationEvolution, MolecularGenomicsHumansMiceModels, MolecularMolecular Sequence DataPhylogenyProtein Interaction Domains and MotifsProtein Structure, TertiarySequence AlignmentConceptsMitochondrial enzymesGenomes of birdsRepresentative vertebrate speciesProtein-protein interactionsAmino acid sequenceVertebrate genomesComparative genomicsMolecular evolutionALDH2 geneEarly vertebratesVertebrate speciesPhylogenetic analysisBioinformatics analysisAcid sequenceMammalian speciesSubunit sequencesBiological aldehydesHuman ALDH2Coenzyme bindingInactivating mutationALDH2 mutantGenesALDH1B1HeterotetramerizationGenome