Cloning and sequence analysis of endoglucanase genes from an industrial fungus, Aspergillus kawachii.
Three endoglucanase genes (cel5A, cel5B, and cel61A) were cloned from an industrial fungus, Aspergillus kawachii. Yeasts transformed with these cDNAs showed endoglucanase activity in medium. Cel5A and Cel61A contained a type 1 cellulose-binding domain (CBD1) at the C-terminus of the enzyme. The putative catalytic regions of Cel5A and Cel5B showed homology with various endoglucanases belonging glycosyl hydrolase family 5 (GH5). Cel5B showed high homology with Cel5A in catalytic region, but it lacked CBD1 and linker. The cel5A contained four introns, whereas cel5B contained five introns. The putative catalytic region of Cel61A showed homology with enzymes belonging to GH61. The cel61A contained no introns.
Hara
Yukari
Y
Department of Molecular Biotechnology, Hiroshima University, Higashi-Hiroshima, Japan.
Hinoki
Yumi
Y
Shimoi
Hitoshi
H
Ito
Kiyoshi
K
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology*; D001483:Base Sequence; D020134:Catalytic Domain; D002480:Cellulase / Q000235:genetics*; D003001:Cloning, Molecular; D017124:Conserved Sequence; D006026:Glycoside Hydrolases / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid
D006026:Glycoside Hydrolases; D002480:Cellulase