Purification, subunit structure and partial amino-acid sequence of anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from the enteric bacterium Serratia marcescens.
The enzyme anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from Serratia marcescens was purified to apparent homogeneity. The purification procedure included ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex gel filtration and hydroxyapatite chromatography. The molecular weight of the native protein as determined on a calibrated Sephadex G-200 column was 45000. Dodecylsulfate-polyacrylamide gel electrophoresis in the presence of reducing agent revealed a subunit molecular weight of 43000 +/- 900, suggesting that the enzyme exists as a monomer. The sequence of the amino-terminal 38 residues revealed that three amino amino acids, glutamine (six residues), glutamic acid (five residues) and serine (five residues) comprised 42% of the sequence composition.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000877:Anthranilate Phosphoribosyltransferase / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D010430:Pentosyltransferases / Q000378:metabolism; D012706:Serratia marcescens / Q000201:enzymology*
D000596:Amino Acids; D010430:Pentosyltransferases; D000877:Anthranilate Phosphoribosyltransferase