Abstract
Reduction is coupled to weight gain. One nitrile group of the substrate PreQ0 couples covalently per subunit of the dimeric nitrile reductase from E. coli.
Highlights
Nitrile reductases (NR) have been discovered as participants in the biosynthetic pathway of queuosine, displaying an unusual activity
The nitrile reductase is a NADPH-dependent enzyme which catalyses the reduction of the nitrile group of 7-cyano-7-deazaguanine (PreQ0) to an amino group, 7-aminomethyl-7-deazaguanine (PreQ1) (Scheme 1)
As expected the dimeric structure of EcoNR is essentially not affected by Electronic supplementary information (ESI) and the MS shows the enzyme to occur predominantly as a dimer
Summary
Nitrile reductases (NR) have been discovered as participants in the biosynthetic pathway of queuosine, displaying an unusual activity They are the first enzymes able to catalyse the reduction of a nitrile group to a primary amine.[1] NR has emerged as a potential tool to overcome and replace traditional chemical approaches and harsh conditions needed to accomplish nitrile hydrogenation.[2] The nitrile reductase is a NADPH-dependent enzyme which catalyses the reduction of the nitrile group of 7-cyano-7-deazaguanine (PreQ0) to an amino group, 7-aminomethyl-7-deazaguanine (PreQ1) (Scheme 1). By introducing mutations in the active site of the NR from Escherichia coli (EcoNR) in the positions previously elucidated for VcNR and BsNR, the essential amino acids for the catalytic cycle were confirmed.3c They are shown to be Cys[190], Asp[197] and His[229] in the schematic representation of the catalytic cycle (Scheme 2)
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