A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria.
The xynC gene from mesophilic Cellulomonas fimi encodes a large 125 kDa modular xylanase (XYLC), consisting of six distinct functional domains. In addition to a single Family 10 catalytic domain, XYLC contains a domain homologous with the nodulation protein, NodB, from nitrogen-fixing bacteria and thermostabilizing and cellulose-binding domains found previously only in xylanases from thermophilic bacteria.
Clarke
J H
JH
Department of Cellular Physiology, Babraham Institute, Cambridge, UK.
Davidson
K
K
Gilbert
H J
HJ
Fontes
C M
CM
Hazlewood
G P
GP
D000192:Actinomycetales / Q000737:chemistry / Q000201:enzymology*; D000595:Amino Acid Sequence; D001665:Binding Sites / Q000502:physiology; D005075:Biological Evolution; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D043364:Endo-1,4-beta Xylanases; D017353:Gene Deletion; D005798:Genes, Bacterial / Q000235:genetics; D006358:Hot Temperature; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid; D014995:Xylosidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D002482:Cellulose; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases