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

Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.

Protein science : a publication of the Protein Society - 1 Nov 2007

Cheriyan Manoj, Toone Eric J, Fierke Carol A

Abstract excerpt

Narrow substrate specificities often limit the use of enzymes in biocatalysis. To further the development of Escherichia coli 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase as a biocatalyst, the molecular determinants of substrate specificity were probed by mutagenesis. Our data demonstrate that S184 is located in the substrate-binding pocket and interacts with the phosphate moiety of KDPG, providing...

Read the complete abstract on PubMed

Topics

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

Share to Aldehyde-Lyases
Share to Aminoglycosides
Share to Catalysis

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

Share to Hydro-Lyases

Share to Models, Chemical

Share to Molecular Conformation

Share to Phosphates

Share to Protein Engineering

Source

Open in PubMed Open full text

Identifiers

PMID: 17962400
DOI: 10.1110/ps.073042907
PMCID: PMC2211689

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

Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates.PMID 17962400Read ↗

Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates.Semantic proximity Read ↗

Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.Semantic proximity Read ↗

Structural basis for substrate specificity in phosphate binding (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12.Semantic proximity Read ↗

The determinants of activity and specificity in actinorhodin type II polyketide ketoreductase.Semantic proximity Read ↗

Enhancement of the substrate scope of transketolase.Semantic proximity Read ↗

A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity.Semantic proximity Read ↗

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Semantic proximity Read ↗

Targeting the role of a key conserved motif for substrate selection and catalysis by 3-deoxy-D-manno-octulosonate 8-phosphate synthase.Semantic proximity Read ↗

Site-directed mutagenesis of aspartic acid 372 at the ATP binding site of yeast phosphoglycerate kinase: over-expression and characterization of the mutant enzyme.Semantic proximity Read ↗

Towards a better understanding of the substrate specificity of the UDP-N-acetylglucosamine C4 epimerase WbpP.Semantic proximity Read ↗

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

Contribution of amino acid side chains to sugar binding specificity in a galactokinase, Gal1p, and a transcriptional inducer, Gal3p.Semantic proximity Read ↗

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