Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-3-21
pubmed:abstractText
The beta-1,4-glycanase Cex of the gram-positive bacterium Cellulomonas fimi is a glycoprotein comprising a C-terminal cellulose-binding domain connected to an N-terminal catalytic domain by a linker containing only prolyl and threonyl (PT) residues. Cex is also glycosylated by Streptomyces lividans. The glycosylation of Cex produced in both C. fimi and S. lividans protects the enzyme from proteolysis. When the gene fragments encoding the cellulose-binding domain of Cex (CBDCex), the PT linker plus CBDCex (PT-CBDCex), and the catalytic domain plus CBDCex of Cex were expressed in S. lividans, only PT-CBDCex was glycosylated. Therefore, all the glycans must be O linked because only the PT linker was glycosylated. A glycosylated form and a nonglycosylated form of PT-CBDCex were produced by S. lividans. The glycosylated form of PT-CBDCex was heterogeneous; its average carbohydrate content was approximately 10 mol of D-mannose equivalents per mol of protein, but the glycans contained from 4 to 12 alpha-D-mannosyl and alpha-D-galactosyl residues. Glycosylated Cex from S. lividans was also heterogeneous. The presence of glycans on PT-CBDCex increased its affinity for bacterial microcrystalline cellulose. The location of glycosylation only on the linker region of Cex correlates with the properties conferred on the enzyme by the glycans.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1066681, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1367716, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1367768, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1368870, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1368939, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1418976, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1427088, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1524674, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1546955, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1572372, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-16347376, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1690330, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1886523, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1904063, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1907435, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-1938913, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2011537, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2123862, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2204153, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2327987, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2656632, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2672447, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2673008, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2681184, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2910842, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2985470, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-2987648, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3096205, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3096818, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3121390, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3134347, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3342887, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3474623, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3600352, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3611052, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-3944078, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-4407487, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-6432782, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-6874701, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-8418047, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-8444787, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-8457214, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-8515228, http://linkedlifedata.com/resource/pubmed/commentcorrection/8106343-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
999-1008
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Streptomyces lividans glycosylates the linker region of a beta-1,4-glycanase from Cellulomonas fimi.
pubmed:affiliation
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't