Linked Life Data

1761533

Source:http://linkedlifedata.com/resource/pubmed/id/1761533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1992-2-7
pubmed:abstractText
Chemotaxis of the marine bacterium Vibrio furnissii to chitin oligosaccharides has been described (Bassler, B. L., Gibbons, P. J., Yu, C., and Roseman, S. (1991) J. Biol. Chem. 266, 24268-24275). Some steps in catabolism of the oligosaccharides are reported here. GlcNAc, (GlcNAc)2, and (GlcNAc)3 are very rapidly consumed by intact cells, about 320 nmol of GlcNAc equivalents/min/mg of protein. (GlcNAc)4 is utilized somewhat more slowly. During these processes, there is virtually no release of hydrolysis products by the cells. The oligosaccharides enter the periplasmic space (via specific porins?) and are hydrolyzed by a unique membrane-bound endoenzyme (chitodextrinase) and an exoenzyme (N-acetyl-beta-glucosaminidase; beta-Glc-NAcidase). The genes encoding these enzymes have been cloned and expressed in Escherichia coli. The chitodextrinase cleaves soluble oligomers, but not chitin, to the di- and trisaccharides, while the periplasmic beta-GlcNAcidase hydrolyzes the GlcNAc termini from the oligomers. The end products in the periplasm, GlcNAc and (GlcNAc)2 (possibly (GlcNAc)3) are catabolized as follows. (a) Disaccharide pathway, A (GlcNAc)2 permease is apparently expressed by Vibrio furnissii. Translocated (GlcNAc)2 is rapidly hydrolyzed by a soluble, cytosolic beta-GlcNAcidase, and the GlcNAc is phosphorylated by an ATP-dependent, constitutive kinase to GlcNAc-6-P. (b) Monosaccharide pathway, Periplasmic GlcNAc is taken up by Enzyme IINag of the phosphoenolpyruvate:glycose phosphotransferase system, yielding GlcNAc-6-P, the common intermediate for both pathways. Finally, GlcNAc-6-P----Ac- + GlcNH2-6-P----Fru-6-P + NH3. (GlcNAc)2 is probably the "true" inducer of the chitin degradative enzymes described in this report and, depending on its concentration in the growth medium, differentially induces the periplasmic and cytosolic beta-GlcNAcidases. The disaccharide pathway appears to be the most important when the cells are confronted with low concentrations of the oligomers (e.g. in chemotaxis swarm plates). The relative activities of the induced enzymes suggest that the rate-limiting steps in oligosaccharide catabolism are the glycosidase activities in the periplasm.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24276-86
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii.
pubmed:affiliation
McCollum-Pratt Institute, Johns Hopkins University, Baltimore, Maryland 21218.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't