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

Determinants of Cofactor Specificity for the Glucose-6-Phosphate Dehydrogenase from Escherichia coli: Simulation, Kinetics and Evolutionary Studies.

PloS one - 1 Jan 2016

Fuentealba Matias, Muñoz Rodrigo, Maturana Pablo, Krapp Adriana, Cabrera Ricardo

Abstract excerpt

Glucose 6-Phosphate Dehydrogenases (G6PDHs) from different sources show varying specificities towards NAD+ and NADP+ as cofactors. However, it is not known to what extent structural determinants of cofactor preference are conserved in the G6PDH family. In this work, molecular simulations, kinetic characterization of site-directed mutants and phylogenetic analyses were used to study the structural basis for the...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bayes Theorem

Share to Escherichia coli Proteins

Share to Glucosephosphate Dehydrogenase

Share to Molecular Dynamics Simulation

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 27010804
DOI: 10.1371/journal.pone.0152403
PMCID: PMC4807051

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Determinants of Cofactor Specificity for the Glucose-6-Phosphate Dehydrogenase from Escherichia coli: Simulation, Kinetics and Evolutionary Studies.PMID 27010804Read ↗

Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases.Semantic proximity Read ↗

Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity.Semantic proximity Read ↗

Investigating effect of mutation on structure and function of G6PD enzyme: a comparative molecular dynamics simulation study.Semantic proximity Read ↗

Understanding the impact of the cofactor swapping of isocitrate dehydrogenase over the growth phenotype of Escherichia coli on acetate by using constraint-based modeling.Semantic proximity Read ↗

Cofactor modification analysis: a computational framework to identify cofactor specificity engineering targets for strain improvement.Semantic proximity Read ↗

Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity.Semantic proximity Read ↗

Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.Semantic proximity Read ↗

Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.Semantic proximity Read ↗

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Cofactor activation and substrate binding in pyruvate decarboxylase. Insights into the reaction mechanism from molecular dynamics simulations.Semantic proximity Read ↗

The β2αB loop determines NAD(P) cofactor specificity and kinetics in trypanosomal D-3-hydroxybutyrate dehydrogenases.Semantic proximity Read ↗

Role of a remote leucine residue in the catalytic function of polyol dehydrogenase.Semantic proximity Read ↗

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