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Non‐Heme Hydroxylase Engineering For Simple Enzymatic Synthesis of L ‐ threo ‐Hydroxyaspartic Acid
Author(s) -
Strieker Matthias,
Essen LarsOliver,
Walsh Christopher T.,
Marahiel Mohamed A.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700557
Subject(s) - hydroxylation , stereospecificity , chemistry , substrate (aquarium) , stereochemistry , heme , protein engineering , asparagine , enzyme , aspartic acid , cytochrome p450 , combinatorial chemistry , biochemistry , catalysis , amino acid , biology , ecology
The direct hydroxylation of aliphatic carbon atoms is a challenging task in organic chemistry. Nature's unique ability to solve this problem by using non‐heme iron hydroxylases was applied to the stereospecific synthesis of the medically important compound L ‐ threo ‐hydroxyaspartic acid. We switched the substrate specificity of a hydroxylase (AsnO) from L ‐asparagine to L ‐aspartic acid by a simple side chain swap in the substrate binding pocket.
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