Cloning and expression of the putative gene coding for GTP cyclohydrolase I from Escherichia coli.
The putative gene coding for GTP cyclohydrolase I of Escherichia coli was isolated from a lambda gt11 expression vector library by using antibodies as a probe and has been subcloned on a 3.8 kb Bam HI fragment in the plasmid vector pUC13. E. coli cells carrying the recombinant plasmid designated pCYH express 100-fold increased levels of the enzyme. The protein formed under the control of the plasmid appears electrophoretically and immunochemically identical with the wild type enzyme.
Katzenmeier
G
G
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Garching, F.R.G.
Schmid
C
C
Bacher
A
A
D000619:Aminohydrolases / Q000235:genetics*; D016667:Bacterial Capsules; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D006136:GTP Cyclohydrolase / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D010957:Plasmids; D011135:Polysaccharides, Bacterial / Q000235:genetics*; D015183:Restriction Mapping
D011135:Polysaccharides, Bacterial; C063323:capsular polysaccharide K4; D000619:Aminohydrolases; D006136:GTP Cyclohydrolase