RT Journal Article SR Electronic(1) A1 Bronnenmeier, Karin A1 Kundt, Kerstin A1 Riedel, Kathrin A1 Schwarz, Wolfgang H. A1 Staudenbauer, Walter L.YR 1997 T1 Structure of the Clostridium stercorarium gene celY encoding the exo-1,4-�-glucanase Avicelase II JF Microbiology, VO 143 IS 3 SP 891 OP 898 DO https://doi.org/10.1099/00221287-143-3-891 PB Microbiology Society, SN 1465-2080, AB 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)., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-143-3-891