Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Alteration of substrate specificity of Zymomonas mobilis alcohol dehydrogenase-2 using in vitro random mutagenesis.

Protein expression and purification - 1 Feb 1997

Rellos P, Ma J, Scopes R K

Abstract excerpt

Random mutagenesis of the gene encoding Zymomonas mobilis alcohol dehydrogenase-2 has enabled isolation of variants of the enzyme that have substrate specificities different from that of the wild-type enzyme. After amino acids responsible for the changes were identified, directed mutation at these sites was also carried out. Variants that are active on butanol have been investigated in detail. Changes at residue...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alcohol Dehydrogenase
Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Isoenzymes

Share to Mutagenesis

Share to Substrate Specificity

Source

Identifiers

PMID: 9116506
DOI: 10.1006/prep.1996.0673

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alteration of substrate specificity of Zymomonas mobilis alcohol dehydrogenase-2 using in vitro random mutagenesis.PMID 9116506Read ↗

Thermostable variants of Zymomonas mobilis alcohol dehydrogenase obtained using PCR-mediated random mutagenesis.Semantic proximity Read ↗

Engineering the cofactor specificity of an alcohol dehydrogenase via single mutations or insertions distal to the 2'-phosphate group of NADP(H).Semantic proximity Read ↗

Respiratory chain analysis of Zymomonas mobilis mutants producing high levels of ethanol.Semantic proximity Read ↗

In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed.Semantic proximity Read ↗

Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.Semantic proximity Read ↗

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.Semantic proximity Read ↗

Effect of acetic acid on ethanol production by Zymomonas mobilis mutant strains through continuous adaptation.Semantic proximity Read ↗

Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase.Semantic proximity Read ↗

Glyoxylate reductase as versatile enzymatic system for pharmaceutical and medical useSemantic proximity Read ↗

Directed evolution of a formate dehydrogenase for increased tolerance to ionic liquids reveals a new site for increasing the stability.Semantic proximity Read ↗

Structural and mutational studies on an aldo-keto reductase AKR5C3 from Gluconobacter oxydans.Semantic proximity Read ↗

Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.