β-ketoacyl-ACP synthase I of Escherichia coli: Nucleotide sequence of thefabB gene and identification of the cerulenin binding residue
- 1 January 1988
- journal article
- research article
- Published by Springer Nature in Carlsberg Research Communications
- Vol. 53 (6) , 357-370
- https://doi.org/10.1007/bf02983311
Abstract
ThefabB gene of E. coli encoding β-ketoacyl-ACP synthase I has been isolated by complementation and sequenced. The enzyme has been purified and its NH2-terminal residues sequenced. Identification of the active site was accomplished by tagging with3H-cerulenin and radio sequencing of the region. Comparison of the deduced primary structures of thefabB gene product with theFAS2 gene product of Saccharomyces cerevisiae revealed the probable active site in chalcone synthases of higher plants.This publication has 67 references indexed in Scilit:
- Chalcone synthase genes in plants: A tool to study evolutionary relationshipsJournal of Molecular Evolution, 1987
- A novel intercistronic regulatory element of prokaryotic operonsNature, 1982
- Flavanone synthase catalyzes CO2 exchange and decarboxylation of malonyl‐CoAFEBS Letters, 1978
- Reaction of Yeast Fatty Acid Synthetase with IodoacetamideEuropean Journal of Biochemistry, 1977
- Screening λgt Recombinant Clones by Hybridization to Single Plaques in SituScience, 1977
- Specific inhibition of candicidin biosynthesis by the lipogenic inhibitor ceruleninBiochimica et Biophysica Acta (BBA) - General Subjects, 1975
- Genetic Modification of Membrane LipidAnnual Review of Biochemistry, 1975
- Inhibition of fatty acid synthesis by the antibiotic ceruleninBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1973
- Inhibition of fatty acid synthetases by the antibiotic ceruleninBiochemical and Biophysical Research Communications, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970