E. coli galactose-1-phosphate uridyl transferase: N-terminal and C-terminal sequences.
A modified procedure for the purification of E. coli galactose-1-phosphate uridyl transferase (E.C. 2.7.6.12) was developed which reproducibly gives pure enzyme. The purified enzyme was shown to be a dimeric protein with a subunit molecular weight of 41,000 and its amino acid composition and content of free sulfhydryl groups were determined. The N-terminal and C-terminal amino acid sequences were found to be NH2-thr-gln-phe-asn-pro-val-asp and -ser(val leu)-ala-COOH respectively. This N-terminal sequence allowed the identification of the start of the transferase gene in the DNA sequence determined by GRINDLEY. Furthermore it appears to define a nine base intercistronic region between the epimerase and transferase genes.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008722:Methods; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000302:isolation & purification; D009876:Operon; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase / Q000235:genetics / Q000302:isolation & purification
D000596:Amino Acids; D009713:Nucleotidyltransferases; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase