Protein modification, aspartate / -hydroxylase

Proline and lysine hydroxylases are required for the postsynthetic modification of collagen, and proline hydroxylase also for the postsynthetic modification of osteocalcin in bone and the Clq component of complement. Aspartate / -hydroxylase is required for the postsynthetic modification of protein C, the vitamin K-dependent protease which hydrolyzes activated factor V in the blood-clotting cascade. Trimethyllysine and 7-butyrobetaine hydroxylases are required for the synthesis of carnitine. 

L-Asp hydroxylated at the /3-carbon to generate 7a ro-3-hydroxyl-L-aspartic acid has so far only been detected in cinnamycin and the duramycins, lantibiotics produced by actinomycetes. " This modification has also been found in mammalian proteins, such as the vitamin K-dependent protein C, and the epidermal growth factor (EGF)-like domain in human plasma factor IX. Both bovine and human aspartyl-/3-hydroxylases have been purified and characterized and their in vitro hydroxylation activity has been shown using proteins... 

Aspartate (3-hydroxylase is required for the post-synthetic modification of the precursor of protein C, the vitamin K-dependent protease that hydrolyses activated factor V in the blood clotting cascade. 

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See also in sourсe #XX -- [ ]

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