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

Crystal structure of pyruvate kinase from Geobacillus stearothermophilus.

Journal of biochemistry - 1 Sept 2008

Suzuki Kenichiro, Ito Sohei, Shimizu-Ibuka Akiko, Sakai Hiroshi

Abstract excerpt

The pyruvate kinase (PK) from a moderate thermophile, Geobacillus stearothermophilus, is an allosteric enzyme activated by AMP and ribose 5-phosphate but not fructose 1, 6-bisphosphate (FBP), which is a common activator of PKs. It has an extra C-terminal sequence (ECTS), which contains a highly conserved phosphoenolpyruvate (PEP) binding motif, but its function and structure remain unclear. To elucidate the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Monophosphate
Share to Amino Acid Motifs
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Geobacillus stearothermophilus

Share to Kinetics

Share to Protein Conformation

Share to Pyruvate Kinase

Share to Zea mays

Source

Identifiers

PMID: 18511452
DOI: 10.1093/jb/mvn069

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

Crystal structure of pyruvate kinase from Geobacillus stearothermophilus.PMID 18511452Read ↗

Possible structure and function of the extra C-terminal sequence of pyruvate kinase from Bacillus stearothermophilus.Semantic proximity Read ↗

Discovery of novel allosteric effectors based on the predicted allosteric sites for Escherichia coli D-3-phosphoglycerate dehydrogenase.Semantic proximity Read ↗

The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.Semantic proximity Read ↗

Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multienzyme complex.Semantic proximity Read ↗

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.Semantic proximity Read ↗

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Examination of MgATP binding in a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus.Semantic proximity Read ↗

Structures of the Mycobacterium tuberculosis GlpX protein (class II fructose-1,6-bisphosphatase): implications for the active oligomeric state, catalytic mechanism and citrate inhibition.Semantic proximity Read ↗

Structure and allosteric regulation of eukaryotic 6-phosphofructokinases.Semantic proximity Read ↗

Crystal structures of Yersinia enterocolitica salicylate synthase and its complex with the reaction products salicylate and pyruvate.Semantic proximity Read ↗

Evolution of allosteric citrate binding sites on 6-phosphofructo-1-kinase.Semantic proximity Read ↗

Identification of a pyrophosphate-dependent kinase and its donor selectivity determinants.Semantic proximity Read ↗

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