Largen M, Mills S E, Rowe J, Yanofsky C
J Biol Chem. 1978 Jan 25;253(2):409-12.
Anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase was purified from the bacterium Erwinia carotovora, a member of the Enterobacteriaceae. The enzyme was homogeneous according to the criteria of gel electrophoresis and NH2-terminal amino acid sequence analysis. The molecular weight of the enzyme as determined on a calibrated Sephadex G-200 column was 67,000 +/- 2,000. Sodium dodecyl sulfate-polyacrylamide gels gave a subunit molecular weight of 40,000 +/- 1,000, suggesting that the enzyme was a dimer. A comparison of the NH2-terminal sequence of the enzyme with the (previously determined) homologue from Serratia marcescens, a monomer with a molecular weight of 45,000, showed that the larger Serratia subunit came into register with amino acid 14 of the Erwinia subunit. The register for the length of the known overlap, 26 amino acids, was highly conserved.
邻氨基苯甲酸-5-磷酸核糖焦磷酸磷酸核糖基转移酶是从胡萝卜软腐欧文氏菌（肠杆菌科成员）中纯化得到的。根据凝胶电泳和氨基末端氨基酸序列分析标准，该酶是均一的。在经校准的葡聚糖凝胶G-200柱上测定的该酶分子量为67,000±2,000。十二烷基硫酸钠-聚丙烯酰胺凝胶给出的亚基分子量为40,000±1,000，表明该酶是二聚体。将该酶的氨基末端序列与粘质沙雷氏菌（分子量为45,000的单体）的（先前测定的）同源物进行比较，结果表明，较大的沙雷氏菌亚基与欧文氏菌亚基的第14位氨基酸对齐。已知重叠长度为26个氨基酸的对齐方式高度保守。
