Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1995-6-1
pubmed:abstractText
Putative domain--domain interactions of the monomeric bifunctional enzyme indoleglycerol phosphate synthase:phosphoribosyl anthranilate isomerase from Escherichia coli were probed by separating the domains on the gene level and expressing them as monofunctional proteins. The engineered monofunctional enzymes were found to be stable, monomeric proteins with virtually full catalytic activity. In addition, binding of indolyglycerol phosphate to the active site of indoleglycerol phosphate synthase and binding of reduced 1-[(2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate, a competitive inhibitor of both indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase, were almost identical in both the mono- and bifunctional enzymes. Furthermore, no association between the monofunctional enzymes was found, neither in vitro, by sedimentation and gel filtration experiments, nor in vivo, by coexpression of the domains in the same cell. Thus, no selective advantages of the bifunctional enzyme from Escherichia coli over the respective monofunctional enzymes were found on a functional level. However, the phosphoribosyl anthranilate isomerase domain appears to stabilize the indoleglycerol phosphate synthase domain of the bifunctional enzyme from Escherichia coli by interactions that seem to subtly influence the kinetics of ligand binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5419-28
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7727400-Aldose-Ketose Isomerases, pubmed-meshheading:7727400-Amino Acid Sequence, pubmed-meshheading:7727400-Base Sequence, pubmed-meshheading:7727400-Binding Sites, pubmed-meshheading:7727400-Carbohydrate Epimerases, pubmed-meshheading:7727400-Chromatography, Gel, pubmed-meshheading:7727400-Chromatography, Ion Exchange, pubmed-meshheading:7727400-Enzyme Stability, pubmed-meshheading:7727400-Escherichia coli, pubmed-meshheading:7727400-Genes, Bacterial, pubmed-meshheading:7727400-Indole-3-Glycerol-Phosphate Synthase, pubmed-meshheading:7727400-Kinetics, pubmed-meshheading:7727400-Molecular Sequence Data, pubmed-meshheading:7727400-Multienzyme Complexes, pubmed-meshheading:7727400-Mutagenesis, Site-Directed, pubmed-meshheading:7727400-Oligodeoxyribonucleotides, pubmed-meshheading:7727400-Operon, pubmed-meshheading:7727400-Protein Engineering, pubmed-meshheading:7727400-Recombinant Proteins, pubmed-meshheading:7727400-Spectrophotometry, pubmed-meshheading:7727400-Substrate Specificity
pubmed:year
1995
pubmed:articleTitle
Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains.
pubmed:affiliation
Abteilung Biophysikalische Chemie, Biozentrum der Universität Basel, Switzerland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't