Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles

ABSTRACT An increasing number of microbes are being identified that organize catabolic pathways within self-assembling proteinaceous structures known as bacterial microcompartments (BMCs). Most BMCs are characterized by their singular substrate specificity and commonly employ B12-dependent radical m...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Bryan Ferlez, Markus Sutter, Cheryl A. Kerfeld
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	activating enzymes bacterial microcompartments glycyl radical enzyme-associated microcompartments glycyl radical enzymes iron-sulfur proteins electron transfer Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/7599856cafe04959bcd2636313609d45
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:7599856cafe04959bcd2636313609d45
record_format	dspace
spelling	oai:doaj.org-article:7599856cafe04959bcd2636313609d452021-11-15T15:55:14ZGlycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles10.1128/mBio.02327-182150-7511https://doaj.org/article/7599856cafe04959bcd2636313609d452019-02-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02327-18https://doaj.org/toc/2150-7511ABSTRACT An increasing number of microbes are being identified that organize catabolic pathways within self-assembling proteinaceous structures known as bacterial microcompartments (BMCs). Most BMCs are characterized by their singular substrate specificity and commonly employ B12-dependent radical mechanisms. In contrast, a less-well-known BMC type utilizes the B12-independent radical chemistry of glycyl radical enzymes (GREs). Unlike B12-dependent enzymes, GREs require an activating enzyme (AE) as well as an external source of electrons to generate an adenosyl radical and form their catalytic glycyl radical. Organisms encoding these glycyl radical enzyme-associated microcompartments (GRMs) confront the challenge of coordinating the activation and maintenance of their GREs with the assembly of a multienzyme core that is encapsulated in a protein shell. The GRMs appear to enlist redox proteins to either generate reductants internally or facilitate the transfer of electrons from the cytosol across the shell. Despite this relative complexity, GRMs are one of the most widespread types of BMC, with distinct subtypes to catabolize different substrates. Moreover, they are encoded by many prominent gut-associated and pathogenic bacteria. In this review, we will focus on the diversity, function, and physiological importance of GRMs, with particular attention given to their associated and enigmatic redox proteins.Bryan FerlezMarkus SutterCheryl A. KerfeldAmerican Society for Microbiologyarticleactivating enzymesbacterial microcompartmentsglycyl radical enzyme-associated microcompartmentsglycyl radical enzymesiron-sulfur proteinselectron transferMicrobiologyQR1-502ENmBio, Vol 10, Iss 1 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	activating enzymes bacterial microcompartments glycyl radical enzyme-associated microcompartments glycyl radical enzymes iron-sulfur proteins electron transfer Microbiology QR1-502
spellingShingle	activating enzymes bacterial microcompartments glycyl radical enzyme-associated microcompartments glycyl radical enzymes iron-sulfur proteins electron transfer Microbiology QR1-502 Bryan Ferlez Markus Sutter Cheryl A. Kerfeld Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
description	ABSTRACT An increasing number of microbes are being identified that organize catabolic pathways within self-assembling proteinaceous structures known as bacterial microcompartments (BMCs). Most BMCs are characterized by their singular substrate specificity and commonly employ B12-dependent radical mechanisms. In contrast, a less-well-known BMC type utilizes the B12-independent radical chemistry of glycyl radical enzymes (GREs). Unlike B12-dependent enzymes, GREs require an activating enzyme (AE) as well as an external source of electrons to generate an adenosyl radical and form their catalytic glycyl radical. Organisms encoding these glycyl radical enzyme-associated microcompartments (GRMs) confront the challenge of coordinating the activation and maintenance of their GREs with the assembly of a multienzyme core that is encapsulated in a protein shell. The GRMs appear to enlist redox proteins to either generate reductants internally or facilitate the transfer of electrons from the cytosol across the shell. Despite this relative complexity, GRMs are one of the most widespread types of BMC, with distinct subtypes to catabolize different substrates. Moreover, they are encoded by many prominent gut-associated and pathogenic bacteria. In this review, we will focus on the diversity, function, and physiological importance of GRMs, with particular attention given to their associated and enigmatic redox proteins.
format	article
author	Bryan Ferlez Markus Sutter Cheryl A. Kerfeld
author_facet	Bryan Ferlez Markus Sutter Cheryl A. Kerfeld
author_sort	Bryan Ferlez
title	Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
title_short	Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
title_full	Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
title_fullStr	Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
title_full_unstemmed	Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles
title_sort	glycyl radical enzyme-associated microcompartments: redox-replete bacterial organelles
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/7599856cafe04959bcd2636313609d45
work_keys_str_mv	AT bryanferlez glycylradicalenzymeassociatedmicrocompartmentsredoxrepletebacterialorganelles AT markussutter glycylradicalenzymeassociatedmicrocompartmentsredoxrepletebacterialorganelles AT cherylakerfeld glycylradicalenzymeassociatedmicrocompartmentsredoxrepletebacterialorganelles
_version_	1718427225175359488

Glycyl Radical Enzyme-Associated Microcompartments: Redox-Replete Bacterial Organelles

Ejemplares similares