ArticleMolecular biotechnology2012
Horse liver alcohol dehydrogenase: new perspectives for an old enzyme.
Article in Molecular biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Biocatalytic Production of a Nylon 6 Precursor from Caprolactone in Continuous Flow.ChemSusChem · 2022Article
- Screening methods for enzyme-mediated alcohol oxidation.Scientific reports · 2022Article
- Biocatalytic access to betazole using a one-pot multienzymatic system in continuous flow.Green chemistry : an international journal and green chemistry resource : GC · 2021Article
- An ADH toolbox for raspberry ketone production from natural resources via a biocatalytic cascade.Applied microbiology and biotechnology · 2021Article
- Modeling Alcohol Dehydrogenase Catalysis in Deep Eutectic Solvent/Water Mixtures.Chembiochem : a European journal of chemical biology · 2020Article
- Biosynthesis of l-Sorbose and l-Psicose Based on C-C Bond Formation Catalyzed by Aldolases in an Engineered Corynebacterium glutamicum Strain.Applied and environmental microbiology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The EE subunit of horse liver alcohol dehydrogenase (HLADH-EE) has been subcloned in pRSETb vector to generate a fusion His-tag protein. The migration from a multistep purification protocol for this well-known enzyme to a single-step has been successfully achieved. Several adjustments to the traditional purification procedure for His-tag proteins have been made to retain protein activity. A full characterization of the fusion enzyme has been carried out and compared with the native one. The K (m) for EtOH, NAD and NADH in the His-tag version of HLADH are in line with the ones reported in literature for the native enzyme. A shift in optimal pH activity is also observed. The enzyme retains the same stability and quaternary structure as the wild type and can therefore be easily used instead of the native HLADH for biotechnological applications.
Indexed as
Identifiers
22544564What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.