title: The beta-mannanase from "Caldocellum saccharolyticum" is part of a multidomain enzyme.
abstract: The complete sequence of a beta-mannanase gene from an anaerobic extreme thermophile was determined, and it shows that the expressed protein consists of two catalytic domains and two binding domains separated by spacer regions rich in proline and threonine residues. The amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase. Neither domain shows homology with any other cellulase or hemicellulase sequence at the nucleic acid or protein level.
authors: Department of Cellular & Molecular Biology, University of Auckland, New Zealand.
authors: M D
authors: MD
authors: Gibbs
authors: D J
authors: DJ
authors: Saul
authors: E
authors: E
authors: Lüthi
authors: P L
authors: PL
authors: Bergquist
mesh_terms: D000595:Amino Acid Sequence; D001421:Bacteria, Anaerobic / Q000201:enzymology* / Q000235:genetics*; D001483:Base Sequence; D002480:Cellulase / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D008361:Mannosidases / Q000235:genetics*; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D044902:beta-Mannosidase
chemical_list: D004269:DNA, Bacterial; D009097:Multienzyme Complexes; D008361:Mannosidases; D044902:beta-Mannosidase; D002480:Cellulase