The major component of the cellulosomes of anaerobic fungi from the genus Piromyces is a family 48 glycoside hydrolase.
Sequencing of two cDNAs from the anaerobic fungi Piromyces equi and Piromyces sp. strain E2 revealed that they both encode a glycoside hydrolase (GH) family 48 cellulase, containing two C-terminal fungal dockerin domains. N-terminal sequencing of the major component of the Piromyces multi-enzyme cellulase/hemicellulase complex, termed the cellulosome, showed that these 80 kDa proteins corresponded to the GH family 48 enzyme. These data show for the first time that GH family 48 cellulases are not confined to bacteria, and that bacterial and fungal cellulosomes share the same pivotal component.
Steenbakkers
P J M
PJ
Department of Microbiology, Faculty of Science, University of Nijmegen, Toernooiveld 1, NL-6525 ED Nijmegen, The Netherlands.
Freelove
A
A
Van Cranenbroek
B
B
Sweegers
B M C
BM
Harhangi
H R
HR
Vogels
G D
GD
Hazlewood
G P
GP
Gilbert
H J
HJ
Op den Camp
H J M
HJ
D020134:Catalytic Domain; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D020089:Piromyces / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA
D006026:Glycoside Hydrolases