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Literature summary for 3.4.21.22 extracted from

  • Johnson, D.J.; Langdown, J.; Huntington, J.A.
    Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex (2010), Proc. Natl. Acad. Sci. USA, 107, 645-650.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Factor VIIIa
-
Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Star (DE3) cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 0.25 M ammonium acetate, 19.5% (w/v) PEG 3350 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
antithrombin
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ factor IXa contains a high-affinity Ca2+-binding site Homo sapiens
additional information factor IXa is not a Na+-binding protease Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Factor X + H2O Homo sapiens
-
Factor Xa + ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00740
-
-

Purification (Commentary)

Purification (Comment) Organism
heparin Sepharose column chromatography and Q Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Factor X + H2O
-
Homo sapiens Factor Xa + ?
-
?

Synonyms

Synonyms Comment Organism
factor IXa
-
Homo sapiens
FIXa
-
Homo sapiens

General Information

General Information Comment Organism
malfunction factor IXa deficiency results in hemophilia Homo sapiens
physiological function factor IXa is a critical enzyme for the formation of stable blood clots Homo sapiens