Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme.
Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii.,Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K. Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii. Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142
