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

The role of calcium ions in factor X activation by thrombin E192Q.

The Journal of biological chemistry - 5 Apr 1992

Le Bonniec B F, Guinto E R, Esmon C T

Abstract excerpt

Despite considerable sequence similarities, blood coagulation serine proteases exhibit remarkable specificity with respect to which zymogen they activate. The basis for this specificity presumably involves recognition of a short sequence within the extended binding pocket of the enzyme, other interactions remote from the catalytic groove, and modulation by a definite protein cofactor. In addition, Ca2+ plays a...

Topics

Amino Acid Sequence
Animals
Calcium
Cations, Divalent
Cattle
Electrophoresis, Polyacrylamide Gel
Factor X
Glutamine
Humans
Hydrolysis
Kinetics
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Recombinant Proteins

Serine

Thrombin

Source

Identifiers

PMID: 1551906

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1551906-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of calcium ions in factor X activation by thrombin E192Q.PMID 1551906Read ↗

Asp-70-->Lys mutant of factor X lacks high affinity Ca2+ binding site yet retains function.Semantic proximity Read ↗

Murine thrombin lacks Na+ activation but retains high catalytic activity.Semantic proximity Read ↗

Role of the activation peptide in the mechanism of protein C activation.Semantic proximity Read ↗

Ca2+ Binding to the First Epidermal Growth Factor-like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain BindingSemantic proximity Read ↗

Contribution of residue 192 in factor Xa to enzyme specificity and function.Semantic proximity Read ↗

X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->beta-tryptase transition.Semantic proximity Read ↗

Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X.Semantic proximity Read ↗

Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin.Semantic proximity Read ↗

Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit.Semantic proximity Read ↗

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.Semantic proximity Read ↗

Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR1 or protein C.Semantic proximity Read ↗

Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.Semantic proximity Read ↗

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