{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P05091","secondaryAccessions":["B4DW54","E7EUE5","Q03639","Q6IB13","Q6IV71"],"uniProtkbId":"ALDH2_HUMAN","entryAudit":{"firstPublicDate":"1987-08-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1990-01-01","entryVersion":267,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4065146"}],"value":"Aldehyde dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20000"}],"value":"1.2.1.19"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20000"}],"value":"1.2.1.24"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10631996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16440063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33355142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39075523"}],"value":"1.2.1.3"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P47738"}],"value":"1.2.1.36"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33355142"}],"value":"1.2.1.46"}]},"alternativeNames":[{"fullName":{"value":"ALDH I"}},{"fullName":{"value":"ALDH class 2"},"shortNames":[{"value":"ALDH-2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"4065146"}],"value":"ALDH-E2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25413692"}],"value":"Nitroglycerin reductase ALDH2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16440063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19506075"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22988236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413692"}],"value":"1.7.1.-"}]}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:404"}],"value":"ALDH2"},"synonyms":[{"value":"ALDM"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20000"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16956664"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19506075"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33355142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39075523"}],"value":"Mitochondrial aldehyde dehydrogenase with broad substrate specificity which participates in the detoxification of ethanol-derived acetaldehyde and endogenous aldehydes, including those arising from lipid peroxidation (PubMed:16956664, PubMed:22339434, PubMed:33355142, PubMed:39075523). The reaction mechanism involves a nucleophilic attack on the aldehyde substrate, resulting in formation of a thiohemiacetal intermediate. Subsequent hydride transfer to NAD+, yields a thioester intermediate which is hydrolyzed to the carboxylic acid product through activation of a water molecule by the catalytic glutamate (PubMed:19506075). In vivo, ALDH2 is required for the clearance of formaldehyde, a cytotoxic and carcinogenic endogenous metabolite that induces DNA damage (PubMed:33355142). It also catalyzes the oxidation of 3,4-dihydroxyphenylacetaldehyde (DOPAL), a reactive intermediate of dopamine catabolism, to 3,4-dihydroxyphenylacetate (DOPAC) (PubMed:16956664). ALDH2 may also catalyze the oxidation of 4-aminobutanal (gamma-aminobutyraldehyde) to 4-aminobutanoate (GABA), representing an alternative route for GABA biosynthesis from polyamine catabolism (By similarity). In vitro, ALDH2 catalyzes the oxidation of acrolein, malondialdehyde, and 4-hydroxynonenal (4-HNE) (PubMed:22339434). It also exhibits esterase activity that is enhanced by NAD+ but does not require it, although the physiological relevance of this activity remains unclear (PubMed:19506075)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16440063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19506075"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22988236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413692"}],"value":"ALDH2 also bioactivates the antianginal drug nitroglycerin through denitration, generating nitric oxide (NO) by a mechanism that remains incompletely understood. The generated NO activates the soluble guanylate cyclase/cGMP signaling pathway, which in turn leads to vasorelaxation and relief of angina pectoris"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 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The aldehyde dehydrogenase activity toward 3,4-dihydroxyphenylacetaldehyde (DOPAL) is inhibited by 4-hydroxy-2-nonenal (4HNE) (PubMed:16956664)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":99.0,"unit":"nmol/min/mg","enzyme":"enzyme with (E)-4-hydroxynon-2-enal as substrate (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":229.0,"unit":"nmol/min/mg","enzyme":"enzyme with (E)-4-hydroxynon-2-enal as substrate (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":250.0,"unit":"nmol/min/mg","enzyme":"enzyme with acrolein as substrate (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":89.0,"unit":"nmol/min/mg","enzyme":"enzyme with acrolein as substrate (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":510.0,"unit":"nmol/min/mg","enzyme":"enzyme with malonaldehyde as substrate (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":581.0,"unit":"nmol/min/mg","enzyme":"enzyme with malonaldehyde as substrate (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"velocity":118.0,"unit":"nmol/min/mg","enzyme":"enzyme with nitroglycerin as substrate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22988236"}]},{"velocity":0.2,"unit":"nmol/min/ug","enzyme":"enzyme for the formation of 1,2-dinitroglycerol","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413692"}]},{"velocity":0.09,"unit":"nmol/min/ug","enzyme":"enzyme for the formation of 1,3-dinitroglycerol","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25413692"}]}],"michaelisConstants":[{"constant":26.0,"unit":"uM","substrate":"NAD(+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10631996"}]},{"constant":0.02,"unit":"uM","substrate":"acetaldehyde (at both pH 7.5 and pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19506075"}]},{"constant":0.9,"unit":"uM","substrate":"(E)-4-hydroxynon-2-enal (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":4.4,"unit":"uM","substrate":"(E)-4-hydroxynon-2-enal (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":0.5,"unit":"uM","substrate":"propanal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10631996"}]},{"constant":1.1,"unit":"uM","substrate":"acrolein (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":1.2,"unit":"uM","substrate":"acrolein (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":26.0,"unit":"uM","substrate":"malonaldehyde (at pH 7.4)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":19.0,"unit":"uM","substrate":"malonaldehyde (at pH 9.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22339434"}]},{"constant":8.7,"unit":"uM","substrate":"nitroglycerin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22988236"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10631996"}],"value":"kcat is 190 min(-1) with propanal as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39075523"}],"value":"Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10631996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12795606"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15983043"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22988236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39075523"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16440063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4065146"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P05091-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P05091-2"],"sequenceIds":["VSP_046715"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38297121"}],"value":"In response to mitochondrial stress, the precursor protein is ubiquitinated by the SIFI complex in the cytoplasm before mitochondrial import, leading to its degradation (PubMed:38297121)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16440063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39075523"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6582480"}],"value":"Genetic variation in ALDH2 is responsible for individual differences in responses to drinking alcohol [MIM:610251]. Allele ALDH2*2 is associated with a very high incidence of acute alcohol intoxication in Orientals and South American Indians, as compared to Caucasians (PubMed:39075523, PubMed:6582480). Allele ALDH2*2 is also associated with impaired efficacy of sublingual nitroglycerin in the treatment of angina and heart failure (PubMed:16440063)"}],"commentType":"POLYMORPHISM"},{"commentType":"DISEASE","disease":{"diseaseId":"AMED syndrome, digenic","diseaseAccession":"DI-06008","acronym":"AMEDS","description":"A form of bone marrow failure syndrome, a heterogeneous group of life-threatening disorders characterized by hematopoietic defects in association with a range of variable extra-hematopoietic manifestations. AMEDS is an autosomal recessive, digenic form characterized by childhood onset of bone marrow failure resulting in aplastic anemia, in association with global developmental delay, intellectual disability, and poor overall growth with short stature.","diseaseCrossReference":{"database":"MIM","id":"619151"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33355142"}]},"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33355142"}],"value":"The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. AMEDS patients carry ADH5 biallelic variants and homozygous or heterozygous ALDH2 variant p.Glu504Lys, affecting protein activity. Cellular and animal studies demonstrate that the simultaneous loss of ALDH2 and ADH5 activities leads to an increase of cellular formaldehyde sensitivity and multisystem abnormalities including hematopoietic failure"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the aldehyde dehydrogenase family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA62825.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"CAA68290.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"CAA68290.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and 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