Gronke, Robert S.;
VanDusen, William J.;
Garsky, Victor M.;
Jacobs, John W.;
Sardana, Mohinder K.;
Stern, Andrew M.;
Friedman, Paul A.
Aspartyl β -hydroxylase: In vitro Hydroxylation of a Synthetic Peptide Based on the Structure of the First Growth Factor-Like Domain of Human Factor IX
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Media type:
E-Article
Title:
Aspartyl β -hydroxylase: In vitro Hydroxylation of a Synthetic Peptide Based on the Structure of the First Growth Factor-Like Domain of Human Factor IX
Contributor:
Gronke, Robert S.;
VanDusen, William J.;
Garsky, Victor M.;
Jacobs, John W.;
Sardana, Mohinder K.;
Stern, Andrew M.;
Friedman, Paul A.
Published:
National Academy of Sciences of the United States of America, 1989
Published in:
Proceedings of the National Academy of Sciences of the United States of America, 86 (1989) 10, Seite 3609-3613
Language:
English
ISSN:
0027-8424
Origination:
Footnote:
Description:
β -Hydroxylation of aspartic acid is a posttranslational modification that occurs in several vitamin K-dependent coagulation proteins. By use of a synthetic substrate comprised of the first epidermal growth factor-like domain in human factor IX and either mouse L-cell extracts or rat liver microsomes as the source of enzyme, in vitro aspartyl β -hydroxylation was accomplished. Aspartyl β -hydroxylase appears to require the same cofactors as known α -ketoglutarate-dependent dioxygenases. The hydroxylation reaction proceeds with the same stereospecificity and occurs only at the aspartate corresponding to the position seen in vivo. Further purification and characterization of this enzymatic activity should now be possible.