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Identification of a PLP‐Dependent Threonine Transaldolase: A Novel Enzyme Involved in 4‐Fluorothreonine Biosynthesis in Streptomyces cattleya
Author(s) -
Murphy Cormac D.,
O'Hagan David,
Schaffrath Christoph
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20011203)40:23<4479::aid-anie4479>3.0.co;2-1
Subject(s) - biochemistry , enzyme , biosynthesis , threonine , transaldolase , pyridoxal phosphate , streptomyces , chemistry , biology , stereochemistry , serine , cofactor , bacteria , pentose phosphate pathway , genetics , glycolysis
The final enzyme on the biosynthetic pathway to 4‐fluorothreonine is identified in Streptomyces cattleya. The enzyme catalyzes a pyridoxal phosphate‐dependent “transaldose” reaction between L ‐threonine and fluoroacetaldehyde (see scheme; PLP=pyridoxal 5′‐phosphate). Unlike threonine aldolases, glycine is not a substrate for this new type of enzyme.