Molecular characterization of a Rhodotorula-lytic enzyme from Paecilomyces lilacinus having beta-1,3-mannanase activity.
We cloned the gene and corresponding cDNA for an extracellular Rhodotorula-lytic enzyme which has beta-1,3-mannase activity, tentatively named MAN5C, from Paecilomyces lilacinus. MAN5C showed a high homology score with the members of glycoside hydrolase family 5 in a domain search with the Pfam database, indicating that MAN5C is a novel and unique member of glycoside hydrolase family 5.
Sugino
Hiroyuki
H
Department of Applied Life Science, Faculty of Engineering, Sojo University. Ikeda, Kumamoto, Japan. hsugino@life.sojo-u.ac.jp
Furuichi
Shinya
S
Murao
Sawao
S
Arai
Motoo
M
Fujii
Takao
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D008351:Mannans / Q000378:metabolism; D008969:Molecular Sequence Data; D010143:Paecilomyces / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D012248:Rhodotorula / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D044902:beta-Mannosidase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
D018076:DNA, Complementary; D008351:Mannans; D044902:beta-Mannosidase