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Investigation of the Radical SAM Enzyme CDG Synthase
Author(s) -
Bruender Nathan,
Dowling Daniel,
Drennan Catherine,
Bandarian Vahe
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.572.12
Subject(s) - stereochemistry , chemistry , enzyme , moiety , biochemistry , atp synthase , active site
7‐Deazapurine containing secondary metabolites and hypermodified tRNA bases are produced in a variety of marine and terrestrial organisms. Although these 7‐deazapurines vary in both their structure and biological roles, they share a common precursor, 7‐cyano‐7‐deazaguanine (preQ 0 ), which is derived from GTP through the action of four enzymes. CDG synthase (QueE) catalyzes the penultimate step, which generates the 7‐deazapurine moiety. QueE is a member of the radical S ‐adenosyl‐L‐methionine (SAM) superfamily and catalyzes a complex radical‐mediated ring contraction to convert 6‐carboxy‐5,6,7,8‐tetrahydropterin (CPH 4 ) into 7‐carboxydeazaguanine (CDG). This paper will discuss the structure function relationships that are emerging from studies of this fascinating transformation. This work was supported by NIH grant GM72623 to VB.