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

Carboxylic acid reductase enzymes (CARs).

Current opinion in chemical biology - 1 Apr 2018

Winkler Margit

Abstract excerpt

Carboxylate reductases (CARs) are emerging as valuable catalysts for the selective one-step reduction of carboxylic acids to their corresponding aldehydes. The substrate scope of CARs is exceptionally broad and offers potential for their application in diverse synthetic processes. Two major fields of application are the preparation of aldehydes as end products for the flavor and fragrance sector and the...

Read the complete abstract on PubMed

Topics

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

Share to Acids
Share to Aldehydes
Share to Biocatalysis

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

Share to Oxidation-Reduction

Share to Oxidoreductases

Share to Protein Conformation

Share to Recombinant Proteins

Share to Substrate Specificity

Source

Identifiers

PMID: 29127833
DOI: 10.1016/j.cbpa.2017.10.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Carboxylic acid reductase enzymes (CARs).PMID 29127833Read ↗

Carbon–carbon double-bond reductases in natureSemantic proximity Read ↗

Bacterial lipoxygenases: Biochemical characteristics, molecular structure and potential applicationsSemantic proximity Read ↗

Nucleophile Promiscuity of Natural and Engineered Aldolases.Semantic proximity Read ↗

Computation-driven redesign of an NRPS-like carboxylic acid reductase improves activity and selectivity.Semantic proximity Read ↗

Structure, function and regulation of carboxylesterasesSemantic proximity Read ↗

Oxidosqualene cyclase second-sphere residues profoundly influence the product profile.Semantic proximity Read ↗

Mechanism-Based Post-Translational Modification and Inactivation in Terpene Synthases.Semantic proximity Read ↗

Substrate ambiguity and catalytic promiscuity within a bacterial proteome probed by an easy phenotypic screen for aldehydes.Semantic proximity Read ↗

Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.Semantic proximity Read ↗

An Ehrlich-inspired retrobiosynthesis of pharmaceutical scaffoldsSemantic proximity Read ↗

Ground-State Electron Transfer as an Initiation Mechanism for Biocatalytic C-C Bond Forming Reactions.Semantic proximity Read ↗

Novel dehydrogenase catalyzes oxidative hydrolysis of carbon-nitrogen double bonds for hydrazone degradation.Semantic proximity Read ↗

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