Title : Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation.

Pub. Date : 2000 Jul 28

PMID : 10801821






6 Functional Relationships(s)
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1 In TAFI activation, however, alanine mutations cause a 50% reduction at Tyr-337, 67% reductions at Asp-338 and Leu-339, and 90% or greater reductions at Val-340, Asp-341, and Glu-343. Alanine carboxypeptidase B2 Homo sapiens
2 In TAFI activation, however, alanine mutations cause a 50% reduction at Tyr-337, 67% reductions at Asp-338 and Leu-339, and 90% or greater reductions at Val-340, Asp-341, and Glu-343. Aspartic Acid carboxypeptidase B2 Homo sapiens
3 In TAFI activation, however, alanine mutations cause a 50% reduction at Tyr-337, 67% reductions at Asp-338 and Leu-339, and 90% or greater reductions at Val-340, Asp-341, and Glu-343. Glutamic Acid carboxypeptidase B2 Homo sapiens
4 A mutation at Asp-349 in the peptide connecting EGF3 to EGF4 eliminated activity against both TAFI and protein C. Oxidation of Met-388 in the peptide connecting EGF5 to EGF6 reduced the rate of protein C activation by 80% but marginally, if at all, affected the rate of TAFI activation. Aspartic Acid carboxypeptidase B2 Homo sapiens
5 A mutation at Asp-349 in the peptide connecting EGF3 to EGF4 eliminated activity against both TAFI and protein C. Oxidation of Met-388 in the peptide connecting EGF5 to EGF6 reduced the rate of protein C activation by 80% but marginally, if at all, affected the rate of TAFI activation. Aspartic Acid carboxypeptidase B2 Homo sapiens
6 Mutation at Phe-376 severely reduced protein C activation but only marginally influenced that of TAFI. Phenylalanine carboxypeptidase B2 Homo sapiens