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

Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate Carboxykinase.

Biochemistry - 26 Jan 2016

Johnson Troy A, Mcleod Matthew J, Holyoak Todd

Abstract excerpt

Phosphoenolpyruvate carboxykinase (PEPCK) is an essential metabolic enzyme operating in the gluconeogenesis and glyceroneogenesis pathways. Previous work has demonstrated that the enzyme cycles between a catalytically inactive open state and a catalytically active closed state. The transition of the enzyme between these states requires the transition of several active site loops to shift from mobile, disordered...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Phosphoenolpyruvate Carboxykinase (GTP)

Share to Pyruvic Acid

Share to Thermodynamics

Source

Identifiers

PMID: 26709450
DOI: 10.1021/acs.biochem.5b01215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate Carboxykinase.PMID 26709450Read ↗

Kinetic and structural analysis of Escherichia coli phosphoenolpyruvate carboxykinase mutants.Semantic proximity Read ↗

Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding.Semantic proximity Read ↗

An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.Semantic proximity Read ↗

Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Semantic proximity Read ↗

Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.Semantic proximity Read ↗

Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit.Semantic proximity Read ↗

Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.Semantic proximity Read ↗

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.Semantic proximity Read ↗

Substrate binding to fluorescent labeled wild type, Lys213Arg, and HIS233Gln Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases.Semantic proximity Read ↗

Aromatic residues in mobile regions distal to the active site support the closed conformation of <i>E. coli</i> DXPSSemantic proximity Read ↗

Thermodynamic dissection of large-scale domain motions coupled with ligand binding of enzyme I.Semantic proximity Read ↗

Examining the role of intersubunit contacts in catalysis by 3-deoxy-d-manno-octulosonate 8-phosphate synthase.Semantic proximity Read ↗

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