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Novel catalytic activity of nitrile hydratase from Rhodococcus sp. N771

Paper ID Volume ID Publish Year Pages File Format Full-Text
21657 43233 2008 6 PDF Available
Title
Novel catalytic activity of nitrile hydratase from Rhodococcus sp. N771
Abstract

Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme catalyzing the hydration of various nitriles to the corresponding amides. We report a novel catalytic activity of NHase. When NHase was incubated with an large excess of commercially available isovaleronitrile, the charge transfer band from the sulfur ligand to the Fe atom shifted from 710 nm to 820 nm, but recovered within 4 min. Similar UV-Vis absorption changes were observed after the addition of isobutylisonitrile (iBuNC), a major impurity in commercially available isovaleronitrile, suggesting that NHase catalyzes the conversion of iBuNC to other compounds. The reaction product was identified as isobutylamine (iBuNH2) by liquid chromatography tandem mass spectrometry. NHase also converts t-butylisonitrile and 1,1,3,3,-tetramethylbutylisonitrile to the corresponding amines. Kinetic analysis of the conversion of iBuNC to iBuNH2 showed a Km value comparable to that for nitriles, while the Vmax value was more than 105 times smaller than that for methacrylonitrile. This is the first report suggesting that NHase is a bifunctional enzyme catalyzing a reaction other than the hydration of nitriles.

Keywords
nitrile hydratase; non-heme iron; isonitrile; amine; bifunctional enzyme
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Novel catalytic activity of nitrile hydratase from Rhodococcus sp. N771
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 2, August 2008, Pages 174–179
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us