Annotation inferences using phylogenetic trees
Toward aldehyde and alkane production by removing aldehyde reductase activity in Escherichia coli.
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Purified YbbO is a strictly NADPH-dependent aldehyde reductase active on C2-C10 aldehydes, highest on hexanal and octanal, about 10-fold less active than DkgA and YahK.
"The other three enzymes GldA, YbbO, and YghA showed about 10-fold lower activity for any of the tested substrates than DkgA and YahK."
Identification of long chain specific aldehyde reductase and its use in enhanced fatty alcohol production in E. coli.
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YbbO is the main E. coli reductase for long-chain fatty aldehydes; kinetics C6-C18 with best affinity for C18 and best efficiency for C16.
"We found that deletion of ybbO gene, which encodes NADP(+) dependent aldehyde reductase, led to >90% reduction in long chain fatty alcohol production."
Selective retinol production by modulating the composition of retinoids from metabolically engineered E. coli.
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Retinol formation in retinal-producing E. coli is due to ybbO, and ybbO overexpression increases the retinol fraction.
"Retinol was produced by the ybbO gene of E. coli which encodes oxidoreductase"
Microbial Production of Bioactive Retinoic Acid Using Metabolically Engineered Escherichia coli.
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Deleting ybbO prevents reduction of retinal to retinol and raises retinoic acid titres.
"deletion of the ybbO gene, which decreased retinoic acid titer through the reduction of retinal to retinol"
Efficient biosynthesis of retinal from Escherichia coli by metabolic engineering.
Selective production of retinol by engineered Saccharomyces cerevisiae through the expression of retinol dehydrogenase.
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Expressed in this yeast strain, E. coli ybbO increases retinol but retinal remains the major product, unlike human RDH12. Conflicts with PMID:39307776, where ybbO was the most active of three screened alcohol dehydrogenases.
"Expression of human RDH10 and Escherichia coli ybbO led to increase in retinol production, but retinal remained as a major product."
[Construction of Saccharomyces cerevisiae cell factories for fermentation production of retinol].
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Among three alcohol dehydrogenases screened on a beta-carotene-producing yeast platform, E. coli ybbO gave the highest retinal-to-retinol conversion (95.6%). Conflicts with PMID:34850377, where retinal remained the major product with ybbO.
"It was determined that ybbO from Escherichia coli exhibited the highest catalytic activity"
Selective biosynthesis of retinol in S. cerevisiae.
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E. coli ybbO is used as a heterologous retinal reductase in yeast retinol production.
"the aldehyde reductase ybbO had been found to increase the retinol proportion in retinoids from 38 to 53% when overexpressed"
Tolerance to Glutaraldehyde in Escherichia coli Mediated by Overexpression of the Aldehyde Reductase YqhD by YqhC.
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ybbO deletion does not affect glutaraldehyde survival; YbbO is not a glutaraldehyde-detoxifying reductase in vivo.
"None of the genes classified as aldehyde reductases (yahK, ybbO, yghA, and ahr) had an impact in glutaraldehyde survival"
ybbO ortholog alignment, orthology and SDR residue analysis (Salmonella vs E. coli)