
Studies on 3‐Deoxy‐ d ‐ arabinoheptulosonate ‐7‐phosphate Synthetase(phe) from Escherichia coli K12
Author(s) -
SIMPSON Richard J.,
DAVIDSON Barrie E.
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb11040.x
Subject(s) - escherichia coli , enzyme , size exclusion chromatography , biochemistry , gel electrophoresis , phosphate , polyacrylamide gel electrophoresis , biology , chemistry , microbiology and biotechnology , chromatography , gene
1 3‐Deoxy‐ d ‐ arabino heptulosonate‐7‐phosphate synthetase(phe) from Escherichia coli K12 has been purified to near homogeneity. The purified enzyme has a specific activity of 67 units mg which is about 1000 times that found in cell‐free extracts of wild type E. coli K12. 2 The minimum molecular weight of the enzyme was estimated by dodecylsulphate‐gel eleetrophoresis to be 33000. Re‐estimation of the native molecular weight by gel filtration confirmed the previously determined value of 110000. 3 Amino acid analysis and tryptic fingerprints indicated that the subunits of the enzyme are very similar and possibly identical. 4 The purified enzyme does not contain Co 2+