Pseudomonas putida tryptophan synthetase.
The two protein components of Pseudomonas putida tryptophan synthetase have been purified to homogeneity. Although there is general similarity between the Pseudomonas enzyme and that of the enteric bacteria, many differences were found. Components from Escherichia coli and P. putida do not stimulate each other enzymatically, and the enzymes differ in their response to monovalent cations. Serine deamination occurs best with the intact enzyme of P. putida, not with the beta(2) subunit alone as in E. coli. The amino acid compositions of the alpha subunits differ appreciably. These findings extend earlier studies showing differences between enteric organisms and pseudomonads in the regulation and genetic organization of the enzymes of the tryptophan pathway.
D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D001322:Autoanalysis; D002499:Centrifugation, Density Gradient; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D003641:Deamination; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000201:enzymology; D005827:Genetics, Microbial; D006358:Hot Temperature; D006836:Hydro-Lyases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D009153:Mutagens; D009154:Mutation; D009604:Nitrosoguanidines; D010710:Phosphates; D011188:Potassium; D011479:Protamines; D011549:Pseudomonas / Q000201:enzymology* / Q000254:growth & development; D011773:Pyruvates / Q000096:biosynthesis; D012694:Serine / Q000378:metabolism; D013045:Species Specificity; D014364:Tryptophan / Q000096:biosynthesis; D014461:Ultracentrifugation
D000596:Amino Acids; D003470:Culture Media; D009153:Mutagens; D009604:Nitrosoguanidines; D010710:Phosphates; D011479:Protamines; D011773:Pyruvates; D012694:Serine; D014364:Tryptophan; D006836:Hydro-Lyases; D011188:Potassium; D000645:Ammonium Sulfate