Linked Life Data

20547376

Source:http://linkedlifedata.com/resource/pubmed/id/20547376

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-9-20
pubmed:abstractText
In insects, ?-N-acetylglucosaminidase (GlcNAcase) participates in critical physiological processes such as fertilization, metamorphosis, and glycoconjugate degradation. Insects produce glycoproteins carrying paucimannosidic-type N-glycans, the terminal GlcNAc residue of which is cleaved by a GlcNAc-linkage specific GlcNAcase, also known as the fused lobes (FDL) protein. To obtain information on the structure of GlcNAcases and insight into their contribution to physiological processes, we cloned Bombyx mori FDL (BmFDL) from silkworm larvae. The full-length cDNA (1.9 kb) encoded a protein of 633 amino acids with 42% amino acid sequence identity to Drosophila melanogaster FDL (DmFDL). Recombinant BmFDL cleaved only ?-1,2-linked GlcNAc residues from the ?-1,3 branch of biantennary N-glycan. This substrate specificity was similar to that of DmFDL. Microsomal FDL activity was inhibited by anti-BmFDL antibodies. Taken together, our results suggest that BmFDL is a N-glycan-processing GlcNAcase in B. mori.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1347-4421
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
386-91
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Cloning and characterization of a ?-N-acetylglucosaminidase (BmFDL) from silkworm Bombyx mori.
pubmed:affiliation
Research Institute of Biological Science, Katakura industries CO., LTD., 1548 Simo-okutomi, Sayama, Saitama 350-1332, Japan. t.nomura@katakura.co.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't