Linked Life Data

3284790

Source:http://linkedlifedata.com/resource/pubmed/id/3284790

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-6-23
pubmed:databankReference
pubmed:abstractText
The genes coding for the enzymes of N-acetylglucosamine (GlcNAc) uptake and metabolism (nagA, nagB, and nagE) are located next to glutaminyl-tRNA synthetase gene (glnS) in the Escherichia coli genome. We determined the nucleotide sequence of the nagE (ptsN) gene, encoding the GlcNAc-specific enzyme II (NagE) of the phosphoenolpyruvate: sugar phosphotransferase system, and the sequence of the putative nagB gene, for glucosamine-6-phosphate deaminase. S1 mapping identified the mRNA transcript for nagE, indicating that nagE might be a sole constituent of the nagE operon, and divergent transcripts which are probably of the nagB, nagA genes. An evaluation of the hydrophobic and hydrophilic properties of NagE shows characteristics of a membrane protein. Also, NagE shows homologies to lactose permease and to the glucose-specific transport protein (enzyme IIGlc), and the glucose-specific phosphoryl carrier protein (enzyme IIIGlc). The latter two homologies are particularly interesting since no enzyme III-like protein for GlcNAc transport has been reported and enzyme IINag is of similar size as the combined enzymes IIGlc plus IIIGlc. This supports the idea that these two transport and phosphorylation systems may have evolved from a common ancestral gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-207
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase.
pubmed:affiliation
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't