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Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophilaCrystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Structural highlights
FunctionNHAA_PSETH 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 PubMedThe crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase. Crystal structure of cobalt-containing nitrile hydratase.,Miyanaga A, Fushinobu S, Ito K, Wakagi T Biochem Biophys Res Commun. 2001 Nov 16;288(5):1169-74. PMID:11700034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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