Literature summary for 3.4.21.5 extracted from

Panizzi, P.; Friedrich, R.; Fuentes-Prior, P.; Richter, K.; Bock, P.E.; Bode, W.
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes (2006), J. Biol. Chem., 281, 1179-1187.

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Application

Application	Comment	Organism
medicine	mechanism of high affinity fibrinogen binding and cleavage in Staphylococcus aureus mediated endocarditis	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
prethrombin 2 bound to a fully active fragment of residues 1-325 from Staphylococcus aureus staphylocoagluase. Complex forms dimers	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	Staphylococcus aureus staphylocoagluase activates proenzyme without proteolysis. Staphylocoagulase-enzyme complex forms a dimer that binds substrate fibrinogen with dissociation constant of 8-34 nM	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Fibrinogen + H2O	-	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	Staphylococcus aureus staphylocoagluase activates proenzyme without proteolysis. Staphylocoagulase-enzyme complex forms a dimer that binds fibrinogen with dissociation constant of 8-34 nM	Homo sapiens

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Release 2023.1 (January 2023)