Structure of the Clostridium stercorarium gene celY encoding the exo-1,4-�-glucanase Avicelase II
Bronnenmeier, Karin and Kundt, Kerstin and Riedel, Kathrin and Schwarz, Wolfgang H. and Staudenbauer, Walter L.,, 143, 891-898 (1997),
doi = https://doi.org/10.1099/00221287-143-3-891,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= The nucleotide sequence of the celY gene coding for the thermostable exo-1,4-�-glucanase Avicelase II of Clostridium stercorarium was determined. The gene consists of an ORF of 2742 bp which encodes a preprotein of 914 amino acids with a molecular mass of 103 kDa. The signal-peptide cleavage site was identified by comparison with the N-terminal amino acid sequence of Avicelase II purified from C. stercorarium. The celY gene is located in close vicinity to the celZ gene coding for the endo-1,4-�-glucanase Avicelase I. The CelY-encoding sequence was isolated from genomic DNA of C. stercorarium with the PCR technique. The recombinant enzyme produced in Escherichia coli as a LacZ'-CelY fusion protein could be purified using a simple two-step procedure. The properties of CelY proved to be consistent with those of Avicelase II purified from C. stercorarium. Sequence comparison revealed that CelY consists of an N-terminal catalytic domain flanked by a domain of 95 amino acids with unknown function joined to a type III cellulose-binding domain. The catalytic domain belongs to the recently proposed family L of cellulases (family 48 of glycosyl hydrolases).,
language=,
type=