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Comparison of the GLA containing zymogens. The figure shows basic structural elements of the GLA-containing zymogens. Each circle is an amino acid.
The prepro leader sequence contains the signal peptide, as well as elements that direct carboxylation of glutamyl residues. Cleavage of the leader
sequence is indicated by showing a slight separation from the mature protein. All have a GLA domain with the GLA residues indicated by filled blue circles.
Prothrombin has a finger loop followed by two Kringle domains. Factors VII, IX, X, and protein C have epidermal growth factor-like domains. Prothrombin,
factor VII, and factor IX circulate as single-chain molecules. Factor X and protein C circulate as two chains that are disulfide linked. All have a catalytic
domain that is homologous between the GLA-containing zymogens. The active site His, Asp, and Ser residues are indicated by the black circles in the
Source: Chapter 115. Molecular Biology and Biochemistry of the Coagulation Factors and Pathways of Hemostasis, Williams Hematology, 8e
catalytic domain. Cleavages that convert the zymogen to an active enzyme are indicated by the arrows. In factor IX, factor X, and protein C, the released
Citation:
Lichtmanby
MA,
TJ,
Seligsohn
Kaushansky
Prchal
JT. Williams
Hematology,
8e; 2010 Available
at:The
http://mhmedical.com/
activation peptide
is indicated
theKipps
yellow
circles.
AfterU,
cleavage,
all ofK,the
molecules
are two-chain
disulfide-linked
molecules.
disulfide connecting
Accessed:
August
03,
2017
the catalytic domain with the rest of the molecule is shown by the heavy bond. All catalytic domains but that of prothrombin remain attached to the GLA
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© 2017 McGraw-Hill Education. All rights reserved
domain following
activation.