Cargando…

Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review

Cellulosimicrobium cellulans (also known with the synonyms Cellulomonas cellulans, Oerskovia xanthineolytica, and Arthrobacter luteus) is an actinomycete that excretes yeast cell wall lytic enzyme complexes containing endo-β-1,3-glucanases [EC 3.2.1.39 and 3.2.1.6] as key constituents. Three genes e...

Descripción completa

Detalles Bibliográficos
Autor principal: Ferrer, Pau
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458353/
https://www.ncbi.nlm.nih.gov/pubmed/16545129
http://dx.doi.org/10.1186/1475-2859-5-10
_version_ 1782127436090048512
author Ferrer, Pau
author_facet Ferrer, Pau
author_sort Ferrer, Pau
collection PubMed
description Cellulosimicrobium cellulans (also known with the synonyms Cellulomonas cellulans, Oerskovia xanthineolytica, and Arthrobacter luteus) is an actinomycete that excretes yeast cell wall lytic enzyme complexes containing endo-β-1,3-glucanases [EC 3.2.1.39 and 3.2.1.6] as key constituents. Three genes encoding endo-β-1,3-glucanases from two C. cellulans strains have been cloned and characterised over the past years. The βglII and βglII(A )genes from strain DSM 10297 (also known as O. xanthineolytica LL G109) encoded proteins of 40.8 and 28.6 kDa, respectively, whereas the β-1,3-glucanase gene from strain ATCC 21606 (also known as A. luteus 73–14) encoded a 54.5 kDa protein. Alignment of their deduced amino acid sequences reveal that βglII and βglII(A )have catalytic domains assigned to family 16 of glycosyl hydrolases, whereas the catalytic domain from the 54.5 kDa glucanase belongs to family 64. Notably, both βglII and the 54.5 kDa β-1,3-glucanase are multidomain proteins, having a lectin-like C-terminal domain that has been assigned to family 13 of carbohydrate binding modules, and that confers to β-1,3-glucanases the ability to lyse viable yeast cells. Furthermore, βglII may also undergo posttranslational proteolytic processing of its C-terminal domain, resulting in a truncated enzyme retaining its glucanase activity but with very low yeast-lytic activity. In this review, the diversity in terms of structural and functional characteristics of the C. cellulans β-1,3-glucanases has been compiled and compared.
format Text
id pubmed-1458353
institution National Center for Biotechnology Information
language English
publishDate 2006
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-14583532006-05-06 Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review Ferrer, Pau Microb Cell Fact Review Cellulosimicrobium cellulans (also known with the synonyms Cellulomonas cellulans, Oerskovia xanthineolytica, and Arthrobacter luteus) is an actinomycete that excretes yeast cell wall lytic enzyme complexes containing endo-β-1,3-glucanases [EC 3.2.1.39 and 3.2.1.6] as key constituents. Three genes encoding endo-β-1,3-glucanases from two C. cellulans strains have been cloned and characterised over the past years. The βglII and βglII(A )genes from strain DSM 10297 (also known as O. xanthineolytica LL G109) encoded proteins of 40.8 and 28.6 kDa, respectively, whereas the β-1,3-glucanase gene from strain ATCC 21606 (also known as A. luteus 73–14) encoded a 54.5 kDa protein. Alignment of their deduced amino acid sequences reveal that βglII and βglII(A )have catalytic domains assigned to family 16 of glycosyl hydrolases, whereas the catalytic domain from the 54.5 kDa glucanase belongs to family 64. Notably, both βglII and the 54.5 kDa β-1,3-glucanase are multidomain proteins, having a lectin-like C-terminal domain that has been assigned to family 13 of carbohydrate binding modules, and that confers to β-1,3-glucanases the ability to lyse viable yeast cells. Furthermore, βglII may also undergo posttranslational proteolytic processing of its C-terminal domain, resulting in a truncated enzyme retaining its glucanase activity but with very low yeast-lytic activity. In this review, the diversity in terms of structural and functional characteristics of the C. cellulans β-1,3-glucanases has been compiled and compared. BioMed Central 2006-03-17 /pmc/articles/PMC1458353/ /pubmed/16545129 http://dx.doi.org/10.1186/1475-2859-5-10 Text en Copyright © 2006 Ferrer; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Ferrer, Pau
Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title_full Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title_fullStr Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title_full_unstemmed Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title_short Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: A review
title_sort revisiting the cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox: a review
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1458353/
https://www.ncbi.nlm.nih.gov/pubmed/16545129
http://dx.doi.org/10.1186/1475-2859-5-10
work_keys_str_mv AT ferrerpau revisitingthecellulosimicrobiumcellulansyeastlyticb13glucanasestoolboxareview