Insight into the Maturation Process of the Nitrile Hydratase Active Site.


Journal

Inorganic chemistry
ISSN: 1520-510X
Titre abrégé: Inorg Chem
Pays: United States
ID NLM: 0366543

Informations de publication

Date de publication:
19 Apr 2021
Historique:
pubmed: 30 3 2021
medline: 14 7 2021
entrez: 29 3 2021
Statut: ppublish

Résumé

The metal binding motif of all nitrile hydratases (NHases, EC 4.2.1.84) is highly conserved (CXXCSCX) in the α-subunit. Accordingly, an eight amino acid peptide (VCTLCSCY), based on the metal binding motif of the Co-type NHase from

Identifiants

pubmed: 33779143
doi: 10.1021/acs.inorgchem.0c02924
doi:

Substances chimiques

Ferric Compounds 0
Hydro-Lyases EC 4.2.1.-
nitrile hydratase EC 4.2.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

5432-5435

Auteurs

Irene R A M Ogutu (IRAM)

Department of Chemistry, Colorado School of Mines, Golden, Colorado 80401, United States.
Department of Chemistry, Marquette University, P.O. Box 1881, Milwaukee, Wisconsin 53201-1881, United States.

Richard C Holz (RC)

Department of Chemistry, Colorado School of Mines, Golden, Colorado 80401, United States.
Department of Chemistry, Marquette University, P.O. Box 1881, Milwaukee, Wisconsin 53201-1881, United States.

Brian Bennett (B)

Department of Physics, Marquette University, 1420 W. Clybourn Street, Milwaukee, Wisconsin 53233, United States.

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Classifications MeSH