Annotation inferences using phylogenetic trees
Toward aldehyde and alkane production by removing aldehyde reductase activity in Escherichia coli.
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E. coli YbbO (orthologue of Salmonella ybbO) is a strictly NADPH-dependent aldehyde reductase in vitro, active on C2-C10 aldehydes with highest activity on hexanal and octanal, but about 10-fold less active than DkgA and YahK.
"YbbO showed broad substrate activity toward all the C2–C10 aldehydes with the highest activity toward hexanal and octanal"
Identification of long chain specific aldehyde reductase and its use in enhanced fatty alcohol production in E. coli.
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Deletion of E. coli ybbO abolishes >90% of long-chain fatty alcohol production from fatty aldehydes, and purified YbbO reduces C6-C18 aldehydes with NADP(H), favouring C16-C18.
"Enzyme kinetic study revealed that YbbO has wide substrate specificity ranging from C6 to C18 aldehyde, with maximum affinity and efficiency for C18 and C16 chain length aldehyde, respectively."
ybbO ortholog alignment and SDR motif analysis
OpenScientist sequence-only hypothesis test for ybbO (gene name and accession withheld)
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Given only the sequence, organism and hypothesis, OpenScientist independently concluded that the protein is a classical SDR with intact catalytic machinery and that NADPH-dependent aliphatic aldehyde reductase activity (GO:0008106) is supported by transfer from E. coli YbbO; it judged retinal reduction a promiscuous, non-core activity and the hydroxysteroid dehydrogenase reading a CDD naming artefact.
"Verdict: SUPPORTED (as an evidence-transfer / ISS–ISO curation lead)."