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

Directed Evolution of Branched-Chain α-Keto Acid Decarboxylase for 3-Hydroxypropionic Acid Production in Escherichia coli via Oxaloacetate.

ACS synthetic biology - 19 Sept 2025

Wang Chuang, Olsthoorn René C L, de Groot Huub J M

Abstract excerpt

3-Hydroxypropionic acid (3-HP) serves as a crucial platform chemical with diverse applications across various industries. In this study, the oxaloacetate pathway was utilized for 3-HP production. This pathway involves the decarboxylation of oxaloacetate into malonic semialdehyde, catalyzed by branched-chain α-keto acid decarboxylase (KdcA), which is subsequently reduced to 3-HP by dehydrogenases. Directed...

Read the complete abstract on PubMed

Topics

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

Share to Carboxy-Lyases
Share to Directed Molecular Evolution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Lactic Acid

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 40815161
DOI: 10.1021/acssynbio.5c00267
PMCID: PMC12455653

Genes

HP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Directed Evolution of Branched-Chain α-Keto Acid Decarboxylase for 3-Hydroxypropionic Acid Production in Escherichia coli via Oxaloacetate.PMID 40815161Read ↗

Engineered Oxalate decarboxylase boosts activity and stability for biological applicationsSemantic proximity Read ↗

Metabolic engineering of Escherichia coli for acetaldehyde overproduction using pyruvate decarboxylase from Zymomonas mobilis.Semantic proximity Read ↗

Construction and evolution of an Escherichia coli strain relying on nonoxidative glycolysis for sugar catabolism.Semantic proximity Read ↗

Heterologous Expression of Ketoreductase ChKRED20 Mutant in Pichia pastoris and Bioreductive Production of (R)-1, 3-Butanediol.Semantic proximity Read ↗

Semi-rational design of L-amino acid deaminase for production of pyruvate and D-alanine by Escherichia coli whole-cell biocatalyst.Semantic proximity Read ↗

Saturated mutagenesis of ketoisovalerate decarboxylase V461 enabled specific synthesis of 1-pentanol via the ketoacid elongation cycle.Semantic proximity Read ↗

Systematic screening for catalytic promiscuity in 4-oxalocrotonate tautomerase: enamine formation and aldolase activity.Semantic proximity Read ↗

Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis.Semantic proximity Read ↗

Efficient synthesis of L-malic acid by malic enzyme biocatalysis with CO2 fixation.Semantic proximity Read ↗

In Situ Acetaldehyde Synthesis for Carboligation Reactions.Semantic proximity Read ↗

Rational engineering of ornithine decarboxylase with greater selectivity for ornithine over lysine through protein network analysis.Semantic proximity Read ↗

Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations: mechanism of pyruvate elimination catalyzed by chorismate enzymes.Semantic proximity Read ↗

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