Dioxygenase mutants and use thereof in synthesizing (2S,3R)-3-hydroxypipecolic acid

Abstract

By mutating arginine at position 97 and asparagine at position 43 of a wild type L-proline-3-hydroxylase, a mutated L-proline-3-hydroxylase is obtained. The mutated L-proline-3-hydroxylase comprises a variant of the wild-type L-proline-3-hydroxylase having SEQ ID NO:1, which comprises a substitution of the arginine corresponding to position 97 (R97) of SEQ ID NO:1 and a substitution of the asparagine corresponding to position 43 (N43) of SEQ ID NO:1; wherein the amino acid substituted into the mutated L-proline-3-hydroxylase at position R97 is methionine, and wherein the amino acid substituted into the mutated L-proline-3-hydroxylase at position N43 is selected from the group consisting of threonine (T), alanine (A), valine (V), serine(S), aspartic acid (D), and lysine (K).

Dependencies are inferred from the claim text.