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Factor Xa
From Proteopedia
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Factor X is a vitamin K-dependent glycoprotein that is synthesized in the liver. Zymogen factor X circulates in plasma as a 2 chain molecule composed of a disulfide linked light chain (Mr = 16500) and heavy chain (Mr = 42,000). Factor X is activated to factor Xa by cleavage of the activation peptide. This reaction is catalyzed by factor VIIa-tissue factor (extrinsic Xase complex) and factor IXa-factor VIIIa (intrinsic Xase complex). | Factor X is a vitamin K-dependent glycoprotein that is synthesized in the liver. Zymogen factor X circulates in plasma as a 2 chain molecule composed of a disulfide linked light chain (Mr = 16500) and heavy chain (Mr = 42,000). Factor X is activated to factor Xa by cleavage of the activation peptide. This reaction is catalyzed by factor VIIa-tissue factor (extrinsic Xase complex) and factor IXa-factor VIIIa (intrinsic Xase complex). | ||
| - | Factor Xa, along with | + | Factor Xa, along with factor Va, calcium, and a phospholipid membrane surface form the prothrombinase complex, to cleave prothrombin to its active form, thrombin. |
| + | {{convert||acre|abbr=on}} | ||
==Structure== | ==Structure== | ||
Revision as of 18:02, 24 April 2010
Contents |
Introduction
Factor X is a vitamin K-dependent glycoprotein that is synthesized in the liver. Zymogen factor X circulates in plasma as a 2 chain molecule composed of a disulfide linked light chain (Mr = 16500) and heavy chain (Mr = 42,000). Factor X is activated to factor Xa by cleavage of the activation peptide. This reaction is catalyzed by factor VIIa-tissue factor (extrinsic Xase complex) and factor IXa-factor VIIIa (intrinsic Xase complex).
Factor Xa, along with factor Va, calcium, and a phospholipid membrane surface form the prothrombinase complex, to cleave prothrombin to its active form, thrombin. Template:Convert
Structure
Enzyme Mechanism
General Serine Protease Mechanism
Related Enzymes
Proteopedia Page Contributors and Editors (what is this?)
Jacqueline Gertz, Michal Harel, Alexander Berchansky, David Canner, Jaime Prilusky
