Post-translational modification is essential for catalytic activity of nitrile hydratase

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The Alpha Subunit of Nitrile Hydratase Is Sufficient for Catalytic Activity and Post-Translational Modification

Nitrile hydratases (NHases) possess a mononuclear iron or cobalt cofactor whose coordination environment includes rare post-translationally oxidized cysteine sulfenic and sulfinic acid ligands. This cofactor is located in the α-subunit at the interfacial active site of the heterodimeric enzyme. Unlike canonical NHases, toyocamycin nitrile hydratase (TNHase) from Streptomyces rimosus is a unique...

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Post-translational modifications in nitrile hydratase family

Fe-type nitrile hydratase (NHase) from Rhodococcus sp. N771 has a novel non-heme iron active center with two post-translationally modified cysteine residues, cysteine-sulfenic and -sulfinic acids. The modified residues are involved in the sequence motif, Cys-Xxx-Leu-Cys-Ser-Cys (Xxx = Ser(Fetype)/Thr(Co-type)), which is conserved among all known NHases as well as in the homologous enzyme, thioc...

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Nitrile Hydratase Activity of Nocardia corallina B-276

Nitrile is a functional group that usually is transformed to amides or carboxylic acids under strong reaction conditions in acidic or basic media and high temperatures. Amides have also been prepared from nitriles at room temperature using strong oxidizing agents such as hydrogen peroxide or sodium superoxide in DMSO. On the other hand biocatalytic hydrolysis of nitriles mediated by nitrilase, ...

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Allosteric post-translational modification codes.

Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial...

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Post-translational modification by SUMO.

Post-translational modifications (PTMs) are chemical alterations to a protein following translation, regulating stability and function. Reversible phosphorylation is an example of an important and well studied PTM involved in a number of cellular processes. SUMOylation is another PTM known to modify a large number of proteins and plays a role in various cellular processes including: cell cycle ...

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ژورنال

عنوان ژورنال: Protein Science

سال: 2000

ISSN: 0961-8368,1469-896X

DOI: 10.1110/ps.9.5.1024