Linked Life Data

21062783

Source:http://linkedlifedata.com/resource/pubmed/id/21062783

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-3-14
pubmed:abstractText
Salmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-?-D-chitobioside, 4-nitrophenyl ?-D-N,N',N?-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-?-D-glucosaminide, peptidoglycan or 4-nitrophenyl ?-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the ?-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Gal?1 ? 4GlcNAc?-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1460-2423
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
426-36
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.
pubmed:affiliation
Department of Veterinary Disease Biology, Faculty of Life Sciences, University of Copenhagen, Grønnegårdsvej 15, 1870 Frederiksberg C., Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't