Loading
ADH1B (All-trans-retinol dehydrogenase [NAD(+)] ADH1B) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Oesophageal cancer.
Catalyses the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism. In vitro can also catalyse the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal. Catalyses in the oxidative direction with higher efficiency.
Open Targets scores its association with cancer at 0.59 (direct and indirect evidence; datatypes literature 0.95, genetic association 0.74).
In plain words · ADH1B (All-trans-retinol dehydrogenase [NAD(+)] ADH1B) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Oesophageal cancer.
ADH1B (All-trans-retinol dehydrogenase [NAD(+)] ADH1B) is an enzyme. In the public catalogues the evidence so far is association rather than a proven role. Tied to Oesophageal cancer.
Catalyses the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism.
No product in this corpus aims at ADH1B yet. Inhibitors are shaped to fit the enzyme's active site so the reaction the cancer relies on stops.
First described 1984. Earliest sequence paper UniProt cites for the protein: Hempel et al, Eur. J. Biochem, 1984, "Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme". Source.
Sources: HGNC HGNC:250 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P00325 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000196616 (association with cancer (MONDO_0004992) 0.59; per-cancer scores at or above 0.5: oesophageal cancer 0.56 (GraphQL API, CC0))
Catalyses the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism. In vitro can also catalyse the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal. Catalyses in the oxidative direction with higher efficiency. Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal. Location: Cytoplasm (UniProt). Locus 4q23 (HGNC).
Query for this target: (TITLE:"ADH1B" OR ABSTRACT:"ADH1B" OR TITLE:"alcohol dehydrogenase 1B class I , beta polypeptide" OR ABSTRACT:"alcohol dehydrogenase 1B class I , beta polypeptide" OR TITLE:"All-trans-retinol dehydrogenase [NAD + ] ADH1B" OR ABSTRACT:"All-trans-retinol dehydrogenase [NAD + ] ADH1B" OR TITLE:"ADH2" OR ABSTRACT:"ADH2") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about ADH1B, not a curated reading list.