Structural highlights
2zcf is a 2 chain structure with sequence from "mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| NonStd Res: | , |
| Related: | 1ahj, 2ahj, 2cyz, 2cz0, 2cz1, 2d0q |
| Gene: | nthA ("Mycobacterium erythropolis" Gray and Thornton 1928), nthB ("Mycobacterium erythropolis" Gray and Thornton 1928) |
| Activity: | Nitrile hydratase, with EC number 4.2.1.84 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
[NHAA_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class. [NHAB_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The kcat of alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on Km was not very significant. In both mutants, the alphaCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated alphaQ90N mutant and determined its structure at a resolution of 1.43 A. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and alphaQ90N mutant NHases suggested the importance of the hydrogen bond networks between alphaGln90 and the iron center for the catalytic activity.
Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771.,Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M. Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771. Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455
