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Putrescine Transaminases for the Synthesis of Saturated Nitrogen Heterocycles from Polyamines
Author(s) -
Slabu Iustina,
Galman James L.,
Weise Nicholas J.,
Lloyd Richard C.,
Turner Nicholas J.
Publication year - 2016
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201600075
Subject(s) - bacillus megaterium , imine , putrescine , chemistry , transaminase , pyridoxal phosphate , aldehyde , stereochemistry , cofactor , escherichia coli , organic chemistry , biochemistry , enzyme , bacteria , biology , catalysis , genetics , gene
Putrescine transaminase (pATA; EC 2.6.1.82) catalyzes the transfer of an amino group from terminal diamine donor molecules to keto acid acceptors by using pyridoxal‐5′‐phosphate as a cofactor. The ygjG genes from Escherichia coli K12, Bacillus megaterium , and Bacillus mycoides were successfully cloned and expressed in E. coli BL21(DE3) cells. The three putrescine transaminases were all shown to prefer diaminoalkanes as substrates and thereby generated cyclic imines from the ω‐amino aldehyde intermediates. The addition of a mild chemical reducing agent rapidly reduced the imine intermediate in situ to furnish a range of N ‐heterocycle products. We applied pATA in a biomimetic synthesis of 2,3‐dihydro‐1 H ‐indolizinium‐containing targets, notably the bioactive alkaloid ficuseptine.