Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.B7 extracted from

  • La Bonte, L.; Pavlov, V.; Tan, Y.; Takahashi, K.; Takahashi, M.; Banda, N.; Zou, C.; Fujita, T.; Stahl, G.
    Mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis (2012), J. Immunol., 188, 885-891.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B7

Organism

Organism UniProt Comment Textmining
Mus musculus P98064
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood serum
-
 Mus musculus
-
endothelial cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Phe-Pip-Arg-4-nitroanilide + H2O a chromogenic thrombin substrate, recombinant human mannose-binding lectin alone fails to cleave the substrate, but cleavage is restored when the recombinant enzyme MASP-1 is added to either MASP-1/-3 KO sera or rhMBL Mus musculus D-Phe-Pip-Arg + 4-nitroaniline
-
 ?

Synonyms

Synonyms Comment Organism
MASP-1
-
 Mus musculus

General Information

General Information Comment Organism
metabolism the enzyme is part of the lectin pathway complement cascade, that is part of the innate immune system responsible for the initiation of inflammation and elimination of invading foreign cells Mus musculus
physiological function the mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis, it plays a key role in thrombus formation in vitro and in vivo. Whole blood aggregation demonstrated increased mannose-binding lectin-mannose-binding lectin-associated serine protease complex-dependent platelet aggregation Mus musculus