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

Enzymatic reduction of levulinic acid by engineering the substrate specificity of 3-hydroxybutyrate dehydrogenase.

Bioresource technology - 1 Apr 2013

Yeon Young Joo, Park Hyung-Yeon, Yoo Young Je

Abstract excerpt

Enzymatic reduction of levulinic acid (LA) was performed for the synthesis of 4-hydroxyvaleric acid (4HV)--a monomer of bio-polyester and a precursor of bio-fuels--using 3-hydroxybutyrate dehydrogenase (3HBDH) from Alcaligenes faecalis. Due to the catalytic inactivity of the wild-type enzyme toward LA, engineering of the substrate specificity of the enzyme was performed. A rational design approach with molecular...

Read the complete abstract on PubMed

Topics

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

Share to Alcaligenes
Share to Kinetics
Share to Molecular Docking Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Mutation

Share to Oxidation-Reduction

Share to Protein Engineering

Share to Substrate Specificity

Source

Identifiers

PMID: 23489571
DOI: 10.1016/j.biortech.2013.01.078

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enzymatic reduction of levulinic acid by engineering the substrate specificity of 3-hydroxybutyrate dehydrogenase.PMID 23489571Read ↗

Highly stereoselective biosynthesis of (R)-α-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase.Semantic proximity Read ↗

Efficient production of (R)-2-hydroxy-4-phenylbutyric acid by using a coupled reconstructed D-lactate dehydrogenase and formate dehydrogenase system.Semantic proximity Read ↗

Evolution of Glucose Dehydrogenase for Cofactor Regeneration in Bioredox Processes with Denaturing Agents.Semantic proximity Read ↗

Substrate specificity engineering of leucine dehydrogenase for efficient synthesis of aromatic L-homophenylalanine.Semantic proximity Read ↗

Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine.Semantic proximity Read ↗

Expanding the cofactor range of aldehyde reductase YqhD by mutating key amino acids.Semantic proximity Read ↗

Characterization and site-directed mutation of a novel aldo-keto reductase from Lodderomyces elongisporus NRRL YB-4239 with high production rate of ethyl (R)-4-chloro-3-hydroxybutanoate.Semantic proximity Read ↗

Efficient biomanufacturing of vitamin E succinate in non-aqueous media via synergistic computational evolution and immobilization of lipase.Semantic proximity Read ↗

Exploring Lactobacillus reuteri DSM20016 as a biocatalyst for transformation of longer chain 1,2-diols: Limits with microcompartment.Semantic proximity Read ↗

Efficient production of enantiomerically pure D-phenyllactate from phenylpyruvate by structure-guided design of an engineered D-lactate dehydrogenase.Semantic proximity Read ↗

A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli.Semantic proximity Read ↗

Strengthening the TCA cycle to alleviate metabolic stress due to blocking by-products synthesis pathway in Klebsiella pneumoniae.Semantic proximity Read ↗

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