PMID:1657875
| Citation |
Talarico, TL, Dev, IK, Dallas, WS, Ferone, R and Ray, PH (1991) Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100. J. Bacteriol. 173:7029-32 |
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| Abstract |
The enzymes 7,8-dihydroxymethylpterin-pyrophosphokinase (HPPK) and 7,8-dihydropteroate synthase (DHPS), which act sequentially in the folate pathway, were purified to homogeneity from crude extracts of Escherichia coli MC4100. The enzymes represent less than 0.01% of the total soluble protein. HPPK was purified greater than 10,000-fold; the native enzyme appears to be a monomer with a molecular mass of 25 kDa and a pI of 5.2. DHPS was purified greater than 7,000-fold; the native enzyme has an apparent molecular mass of 52 to 54 kDa and is composed of two identical 30-kDa subunits. The amino-terminal sequences for both enzymes have been determined. |
| Links | |
| Keywords |
Amino Acid Sequence; Dihydropteroate Synthase/isolation & purification; Dihydropteroate Synthase/metabolism; Diphosphotransferases; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Molecular Sequence Data; Phosphotransferases/isolation & purification; Phosphotransferases/metabolism |
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