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

Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate.

Journal of molecular biology - 22 Mar 2002

Scott John W, Norman David G, Hawley Simon A, Kontogiannis Luke, Hardie D Grahame

Abstract excerpt

We have expressed a truncated form of the alpha1 kinase domain of AMP-activated protein kinase (AMPK) in Escherichia coli as a glutathione-S-transferase fusion (GST-KD). A T172D mutant version did not require prior phosphorylation and was utilized for most subsequent studies. We have also created a recombinant substrate (GST-ACC) by expressing 34 residues around the major phosphorylation site (Ser79) on rat...

Read the complete abstract on PubMed

Topics

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

Share to Acetyl-CoA Carboxylase
Share to AMP-Activated Protein Kinases

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

Share to Catalytic Domain

Share to Glutathione Transferase

Share to Histidine

Share to Multienzyme Complexes

Share to Rats, Wistar

Share to Serine

Source

Identifiers

PMID: 11902845
DOI: 10.1006/jmbi.2001.5316

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

Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate.PMID 11902845Read ↗

Distinct structural mechanisms determine substrate affinity and kinase activity of protein kinase Cα.Semantic proximity Read ↗

Structural insight into the autoinhibition mechanism of AMP-activated protein kinase.Semantic proximity Read ↗

Structural basis for compound C inhibition of the human AMP-activated protein kinase α2 subunit kinase domain.Semantic proximity Read ↗

Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit.Semantic proximity Read ↗

Determination of AMP-activated protein kinase phosphorylation sites in recombinant protein expressed using the pET28a vector: a cautionary tale.Semantic proximity Read ↗

Comparison of cAMP-dependent protein kinase substrate specificity in reaction with proteins and synthetic peptides.Semantic proximity Read ↗

Advances in the research of AMPK and its subunit genes.Semantic proximity Read ↗

Structural insights into the architecture and allostery of full-length AMP-activated protein kinase.Semantic proximity Read ↗

Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase.Semantic proximity Read ↗

Structural basis of substrate recognition and translocation by human ABCD1Semantic proximity Read ↗

In vitro mutagenesis studies at the arginine residues of adenylate kinase. A revised binding site for AMP in the X-ray-deduced model.Semantic proximity Read ↗

Distal recognition sites in substrates are required for efficient phosphorylation by the cAMP-dependent protein kinase.Semantic proximity Read ↗

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