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3.4.21.B1: hyaluronan-binding serine protease

This is an abbreviated version!
For detailed information about hyaluronan-binding serine protease, go to the full flat file.

Word Map on EC 3.4.21.B1

Reaction

endopeptidase activity. Cleaves C-terminal site of Lys and Arg =

Synonyms

factor seven activating protease, factor VII activating protease, factor VII-activating protease, FASP, FSAP, gelatinolytic serine proteinase, HABP, HABP2, hyaluronan binding protein 2, hyaluronan-binding protease, hyaluronic acid-binding protease, PHBP, PHBSP, plasma hyaluronan-binding protein, S01.033

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B1 hyaluronan-binding serine protease

General Information

General Information on EC 3.4.21.B1 - hyaluronan-binding serine protease

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the active site residues of a serine proteinase are conserved in the serine protease domain of the enzyme. The enzyme has a similar domain structure and tissue distribution to those of human hyaluronan binding protein 2 (HABP2), putative phylogenetic tree
malfunction
-
the variant Marburg I polymorphism results in low enzymatic activity and is associated with an enhanced risk of carotid stenosis and stroke
metabolism
FSAP is exclusively activated by the positively charged surfaces polyethylenimine and poly-L-lysine, not by the negatively charged glass or self-assembled monolayer with carboxyl group termination or uncharged (Teflon AF) surfaces. Activation is concomitant with coagulation. A contact phase inhibitor diminishes coagulation to background levels for all surfaces except polyethylenimine
physiological function