Biological Nitrile Reduction ‐ Structure and Mechanism (LB136)

Autor: Manal A. Swairjo, Dirk Iwata-Reuyl, Maryam Kiani, Vimbai M. Chikwana, Bobby W.K. Lee
Rok vydání: 2014
Předmět:
Zdroj: The FASEB Journal. 28
ISSN: 1530-6860
0892-6638
DOI: 10.1096/fasebj.28.1_supplement.lb136
Popis: The enzyme QueF catalyzes the NADPH-dependent reduction of the nitrile group of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) in the biosynthesis pathway to the tRNA modified nucleoside Queuosine. The only nitrile reductase known in biology, QueF is a potential new candidate for industrial biocatalysis of nitrile transformations to amines. QueF belongs to the tunneling fold (T-fold) structural superfamily built around a small ββααββ protein domain that oligomerizes to form a β2nαn barrel and facilitates interfacial catalysis of a variety of chemical reactions. In recent years, several crystal structures have been determined of unimodular and bimodular QueF enzymes, and of active site mutants and complexes with substrate and cofactor. Here we present crystal structures and biochemical and transient kinetic data that elucidate the mechanism of biological nitrile reduction and provide insight into the molecular evolution of T-fold mediated interfacial catalysis. Structures of substra...
Databáze: OpenAIRE
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