Open AccessTwo genes of the anaerobic fungus Orpinomyces sp. strain PC‐2 encoding cellulases with endoglucanase activities may have arisen by gene duplication
Author(s) -
Chen Huizhong,
Li XinLiang,
Blum David L,
Ljungdahl Lars G
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb12842.x
Subject(s) - gene , cellulase , open reading frame , biology , complementary dna , biochemistry , homology (biology) , glycosyl , microbiology and biotechnology , genetics , peptide sequence , enzyme
A cDNA designated celE cloned from Orpinomyces PC‐2 consisted of an open reading frame encoding a polypeptide (CelE) of 477 amino acids. CelE was highly homologous to CelBs of Orpinomyces (72.3% identity) and Neocallimastix (67.9% identity) and like them it had a non‐catalytic repeated peptide domain (NCRPD) at the C‐terminal end. The catalytic domain of CelE was homologous to glycosyl hydrolases of Family 5, found in several anaerobic bacteria. The gene of celE was devoid of introns. The recombinant proteins CelE and CelB of Orpinomyces PC‐2 randomly hydrolyzed carboxymethylcellulose and cello‐oligosaccharides in the pattern of endoglucanases. The results indicated that a gene of bacterial origin was duplicated to form celE and celB of Orpinomyces PC‐2.