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

Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism.

Biochimica et biophysica acta - 2 Apr 1998

Brewer J M, Glover C V, Holland M J, Lebioda L

Abstract excerpt

The S39A mutant of yeast enolase (isozyme 1), prepared by site-directed mutagenesis, has a relative Vmax of 0.01% and an activation constant for Mg2+ ca. 10-fold higher, compared with native enzyme. It is correctly folded. There is little effect of solvent viscosity on activity. We think that the...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Phosphopyruvate Hydratase
Share to Saccharomyces cerevisiae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 9602170
DOI: 10.1016/s0167-4838(98)00004-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-9602170-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism.PMID 9602170Read ↗

The H159A mutant of yeast enolase 1 has significant activity.Semantic proximity Read ↗

Preparation by site-directed mutagenesis and characterization of the E211Q mutant of yeast enolase 1.Semantic proximity Read ↗

Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases.Semantic proximity Read ↗

Can the local electric field be a descriptor of catalytic activity? A case study on chorismate mutase.Semantic proximity Read ↗

Engineering the enolase magnesium II binding site: implications for its evolution.Semantic proximity Read ↗

How the N-terminal extremity of Saccharomyces cerevisiae IF1 interacts with ATP synthase: a kinetic approach.Semantic proximity Read ↗

Effects of the G376E and G157D mutations on the stability of yeast enolase--a model for human muscle enolase deficiency.Semantic proximity Read ↗

Alteration of apparent negative cooperativity of ATPase activity by alpha-subunit glutamine 173 mutation in yeast mitochondrial F1. Correlation with impaired nucleotide interaction at a regulatory site.Semantic proximity Read ↗

The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues.Semantic proximity Read ↗

Site-directed mutations of arginine 65 at the periphery of the active site cleft of yeast 3-phosphoglycerate kinase enhance the catalytic activity and eliminate anion-dependent activation.Semantic proximity Read ↗

Aromatic residues in the C-terminal region of glutathione transferase A1-1 influence rate-determining steps in the catalytic mechanism.Semantic proximity Read ↗

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