3.4.21.6: coagulation factor Xa

This is an abbreviated version!
For detailed information about coagulation factor Xa, go to the full flat file.

Reaction

selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin =

Synonyms

activated blood-coagulation factor X, activated factor X, activated Stuart-Prower factor, autoprothrombin C, blood coagulation factor X, blood coagulation factor Xa, blood-coagulation factor X, activated, clotting factor Xa, coagulation factor X, coagulation factor Xa, f.Xa, factor X, factor Xa, Fgl2 protein, fX, FXa, FXaalpha/beta, hXa, More, oscutarin, plasma thromboplastin, procoagulant factor X, prothrombase, prothrombin activator, prothrombinase, Stuart factor, thrombokinase, thromboplastin, thromboplastin, plasma, trocarin, Trocarin prothrombin activator, VAP, Virus activating protease, Xa

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.6 coagulation factor Xa

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Results	in table
63	Activating Compound
192	AA Sequence
25	Application
1	CAS Registry Number
10	Cloned(Commentary)
18	Cofactor
12	Crystallization (Commentary)
17523	Disease/ Diagnostics
6	Expression
30	General Information
1	General Stability
125	IC50 Value
1029	Inhibitors
488	Ki Value [mM]
103	KM Value [mM]
50	Localization
33	Metals/Ions
8	Molecular Weight [Da]
94	Natural Substrates/ Products (Substrates)
214	Organism
307	PDB ID
36	pH Optimum
21	Posttranslational Modification
42	Protein Variants
11	Purification (Commentary)
56	Reaction
2	Reaction Type
214	Reference
139	Source Tissue
10	Specific Activity [micromol/min/mg]
1	Storage Stability
267	Substrates and Products (Substrate)
36	Subunits
290	Synonyms
36	Temperature Optimum [°C]
85	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 3.4.21.6 - coagulation factor Xa

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

Homo sapiens

-

-

754844

no modification

Bos taurus

-

analysis for hexoses, amino sugars and neuraminic acids is negative

81419

proteolytic modification

16 entries

side-chain modification

Bos taurus

-

contains a carbohydrate moiety

81418

proteolytic modification

Bos taurus

-

a protein present in Russell's viper venom specifically cleaves a specific peptide bond, resulting in the release of a glycopeptide of MW 11000 Da from the amino terminal end of the heavy chain

81422

proteolytic modification

Bos taurus

-

autoproteolytic conversion of factor Xaalpha to factor Xabeta by excision of a 4000 Da fragment, beta-peptide

81425

proteolytic modification

Bos taurus

-

the zymogen factor X is converted to its actively enzymatic form by incubation with Russell's viper venom

81419, 81422

proteolytic modification

Bos taurus

-

factor X is the zymogen

81416, 81417

proteolytic modification

Bos taurus

-

processing and activation of the recombinant wild-type and mutant zymogens to mature enzymes by Russell's viper venom

650585

proteolytic modification

Bos taurus

-

the enzyme is processed from factor X to factor Xa

651123

proteolytic modification

Bos taurus

-

the factor X is activated to factor Xa by Russell's viper venom

683178

proteolytic modification

Homo sapiens

-

activation of factor X and GDFX to factor Xa and GDFXa, respectively, by Russel's viper venom and human antithrombin

649955

proteolytic modification

Homo sapiens

-

processing and activation of the recombinant wild-type and mutant zymogens to mature enzymes by Russell's viper venom at 37°C and pH 7.4

650164

proteolytic modification

Homo sapiens

-

processing of factor X to factor Xa can be performed with Russell's viper venom

652278

proteolytic modification

Homo sapiens

-

processing of factor X to factor Xa can be performed with Russell's viper venom at pH 8.3

652262

proteolytic modification

Homo sapiens

P00742

reorientation of the N-terminus of serine protease domain after proteolytic activation of factor X to factor Xa, cleavage of the activation peptide at the Arg194-Ile195 peptide bond

650582

proteolytic modification

Homo sapiens

-

factor Xa formation is catalyzed by the intrinsic tenase, i.e. factor VIIa and tissue factor complex, via proteolytic cleavage, analysis of roles of extrinsic and intrinsic tenases in fX activation, and roles of extrinsic tenase and fXIa in fIX activation during clot formation in a reaction-diffusion system, computational simulations, overview

683259

proteolytic modification

Homo sapiens

-

the factor X is activated to factor Xa by Russell's viper venom

683178

proteolytic modification

Homo sapiens

-

factor X is converted into its active form, factor Xa, in response to the factor VIIa-tissue factor, i.e. thromboplastin, complex, overview. Kinetics of immobilized tissue factor binding to factor VIIa compared to non-immobilzed one, overview. Immobilization of the tissue factor on the surface has no qualitative effect on the kinetics of tissue factor interaction with factor VIIa and does not affect the activation activity of factor Xa and the coagulation cascade

717234

proteolytic modification

Rattus norvegicus

-

activation of the zymogen factor X to factor Xa by proteolytic cleavage initiates the extrinsic coagulation pathway, overview

683838