Revisiting the Cellulosimicrobium cellulans yeast-lytic β-1,3-glucanases toolbox : A review
Ferrer, Pau (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)

Fecha:	2006
Resumen:	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 βglIIA 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 βglIIA 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.
Derechos:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades.
Lengua:	Anglès
Documento:	Article ; Versió publicada
Publicado en:	Microbial cell factories, Vol. 5, N. 10 (March 2006) , p. 1-8, ISSN 1475-2859

DOI: 10.1186/1475-2859-5-10
PMID: 16545129

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