E. coli galactose-1-phosphate uridyl transferase: N-terminal and C-terminal sequences

Mol Cell Biochem. 1979 Feb 9;23(3):167-75. doi: 10.1007/BF00219455.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Methods
  • Molecular Weight
  • Nucleotidyltransferases* / isolation & purification
  • Operon
  • UTP-Hexose-1-Phosphate Uridylyltransferase* / genetics
  • UTP-Hexose-1-Phosphate Uridylyltransferase* / isolation & purification

Substances

  • Amino Acids
  • Nucleotidyltransferases
  • UTP-Hexose-1-Phosphate Uridylyltransferase