Complete sequence of the glt A gene encoding citrate synthase in Escherichia coli

• Published in: Biochemistry (Easton) Vol. 22; no. 23; pp. 5243 - 5249
• Main Authors: NER, S. S, BHAYANA, V, BELL, A. W, GILES, I. G, DUCKWORTH, H. W, BLOXHAM, D. P
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-01-1983
• Subjects: Biological and medical sciences; Escherichia coli; Fundamental and applied biological sciences. Psychology; Genes. Genome; Molecular and cellular biology; Molecular genetics; Bacteria; Primary structure; Citrate (si)-synthase; Gene; Enzyme; Escherichia coli
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00292a001

The sequence of a 3265 base pair HindIII-EcoRI restriction fragment spanning the glt A gene from Escherichia coli was determined. The sequences for initiation and termination of transcription as well as ribosome binding are predicted. The frequency of codon usage within glt A consistent with that expected for a gene which is strongly expressed. Comparison of the structure of E. coli with pig heart citrate synthase revealed strong sequence conservation of residues in the active site. An exception is that E. coli citrate synthase does not contain a residue equivalent to Arg-46 in the pig heart sequence. This residue is implicated in binding the 5'-diphosphate of coenzyme A, and the absence of this feature might contribute to diminished affinity for coenzyme A derivatives and altered regulatory properties of E. coli citrate synthase.