Por favor, use este identificador para citar o enlazar este ítem:
https://doi.org/10.1021/acs.biochem.8b00009
Twittear
Título: | Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea |
Fecha de publicación: | 2018 |
Editorial: | ACS Publications |
Cita bibliográfica: | Biochemistry 2018, 57(7), 1155-1165 |
ISSN: | Print: 0006-2960 Electronic: 1520-4995 |
Materias relacionadas: | CDU::5 - Ciencias puras y naturales::57 - Biología::579 - Microbiología |
Palabras clave: | Amines Genomics Monomers Peptides and proteins Redox reactions |
Resumen: | Glycine oxidase from Pseudoalteromonas luteoviolacea (PlGoxA) is a cysteine tryptophylquinone (CTQ)-dependent enzyme. Sequence and phylogenetic analysis place it in a newly designated subgroup (Group IID) of a recently identified family of LodA-like proteins, which are predicted to possess CTQ. The crystal structure of PlGoxA reveals that it is a homo-tetramer. It possesses an N-terminal domain with no close structural homologues in the Protein Data Bank. The active site is quite small due to intersubunit interactions, which may account for the observed cooperativy towards glycine. Steady-state kinetic analysis yielded values of kcat=6.0±0.2 s−1, K0.5=187±18 μM and h=1.77±0.27. In contrast to other quinoprotein amine dehydrogenases and oxidases that exhibit anomalously large primary kinetic isotope effects on the rate of reduction of the quinone cofactor by the amine substrate, no significant primary kinetic isotope effect was observed for this reaction of PlGoxA. The absorbance spectrum of the glycine-reduced PlGoxA exhibits features in the 400-650 nm range that have not previously been seen in other quinoproteins. Thus, in addition to the unusual structural features of PlGoxA, the kinetic and chemical reaction mechanisms of the reductive half-reaction of PlGoxA appear to be distinct from those of other amine dehydrogenases and amine oxidases that use tryptophylquinone and tyrosylquinone cofactors. |
Autor/es principal/es: | Andreo-Vidal, Andres Mamounis, Kyle J. Sehanobish, Esha Avalos, Dante Campillo-Brocal, Jonatan C. Sanchez-Amat, Antonio Yukl, Erik T. Davidson, Victor L. |
Facultad/Departamentos/Servicios: | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Genética y Microbiología |
URI: | http://hdl.handle.net/10201/138985 |
DOI: | https://doi.org/10.1021/acs.biochem.8b00009 |
Tipo de documento: | info:eu-repo/semantics/article |
Número páginas / Extensión: | 28 |
Derechos: | info:eu-repo/semantics/openAccess Attribution-NonCommercial-NoDerivatives 4.0 Internacional |
Descripción: | Copyright © 2018 American Chemical Society ©<2018>. This manuscript version is made available under the CC-BY-NC 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the, Accepted, version of a Published Work that appeared in final form in Biochemistry. To access the final edited and published work see: https://doi.org/ 10.1021/acs.biochem.8b00009. |
Aparece en las colecciones: | Artículos: Genética y Microbiología |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
nihms953704.pdf | 1,13 MB | Adobe PDF | Visualizar/Abrir |
Este ítem está sujeto a una licencia Creative Commons Licencia Creative Commons