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Literature summary for 3.4.21.22 extracted from

  • Hopfner, K.P.; Lang, A.; Karcher, A.; Sichler, K.; Kopetzki, E.; Barndstetter, H.; Huber, R.; Bode, W.; Engh, R.A.
    Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding (1999), Structure Fold. Des., 7, 989-996.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
of a recombinant two-domain construct of fIXa in complex with p-benzamidine. The 99-loop on Tyr99 plays a major role in substrate interaction, it may be rearranged in the factor X activation complex Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor X + H2O Homo sapiens a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor X + H2O a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa Homo sapiens ?
-
?
factor X + H2O
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Homo sapiens factor Xa
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?
additional information fIXa among the S1 family of serine proteinases is uniquely inefficient against synthetic peptide substrates Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
FIXa
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Homo sapiens