Factor Xa: Difference between revisions
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Bacterial subtilisin serine protease shows no sequence or structural homology to the mammalian serine protease family, but is functionally identical. Subtilisin uses a His, Asp, Ser catalytic triad with the same mechanism of catalysis. This is an example of convergent evolution.<ref name="evolution"/> | Bacterial subtilisin serine protease shows no sequence or structural homology to the mammalian serine protease family, but is functionally identical. Subtilisin uses a His, Asp, Ser catalytic triad with the same mechanism of catalysis. This is an example of convergent evolution.<ref name="evolution"/> | ||
===Light Chain=== | |||
The factor Xa light chain contains a γ-carboxyglutamic acid (Gla) domain [http://en.wikipedia.org/wiki/Gla_domain γ-carboxyglutamic acid (Gla)](11 gla residues) as well as two epidermial growth factor (EGF)-like domains [http://en.wikipedia.org/wiki/Epidermal_growth_factor epidermal growth factor (EGF)].<ref name="EGF">PMID:8355279</ref> The Gla domain is responsible for the high-affinity binding of calcium ions and interactions with phospholipid membrane surfaces. Recent crystal structures suggest that the N-terminal epidermal growth factor (EGF)-like domain is flexibly, while the second EGF domain maintains contacts with the catalytic domain. | |||
===Heavy Chain=== | |||
The factor Xa heavy chain contains the activation peptide and trypsin-like serine protease domain | |||
===Catalytic Triad=== | ===Catalytic Triad=== | ||
