Review
Catalysis in the nitrilase superfamily
Current Opinion in Structural Biology, Vol.12(6), pp.775-782
2002
DOI: 10.1016/S0959-440X(02)00387-1
PMID: 12504683
Abstract
Recently, we defined the nitrilase superfamily as consisting of 12 families of amidases, N-acyltransferases and presumptive amidases, in addition to the family of plant and bacterial nitrilases for which the superfamily was named. A novel Glu-Lys-Cys catalytic triad, found at the crystallographically defined Nit active site of worm NitFhit, was postulated to constitute the catalytic residues for all members of the superfamily. Recent experimental results confirm the essentiality of the catalytic triad residues and specify the biochemical functions of additional branches and sub-branches of the nitrilase superfamily. Most members of the nitrilase superfamily are not nitrilase but rather amidases and N-acyltransferases. Members of the nitrilase superfamily are thiol enzymes that perform an array of carbon-nitrogen bond hydrolysis and condensation reactions in natural products biosynthesis and protein modification.
Details
- Title: Subtitle
- Catalysis in the nitrilase superfamily
- Creators
- Charles Brenner - Structural Biology and Bioinformatics Program, Kimmel Cancer Center, Philadelphia, PA 19107, USA
- Resource Type
- Review
- Publication Details
- Current Opinion in Structural Biology, Vol.12(6), pp.775-782
- Publisher
- Elsevier Ltd
- DOI
- 10.1016/S0959-440X(02)00387-1
- PMID
- 12504683
- ISSN
- 0959-440X
- eISSN
- 1879-033X
- Language
- English
- Date published
- 2002
- Academic Unit
- Biochemistry and Molecular Biology; Internal Medicine
- Record Identifier
- 9983788428902771
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