Di Ilio C, Aceto A, Piccolomini R, Allocati N, Caccuri A M, Barra D, Federici G
Istituto di Scienze Biochimiche, Cattedra di Microbiologia, Università di Chieti, Roma, Italy.
FEBS Lett. 1989 Jun 19;250(1):57-9. doi: 10.1016/0014-5793(89)80684-2.
The N-terminal amino acid sequence of glutathione transferase, Pm-GST-6.0, purified from Proteus mirabilis [(1988) Biochem. J. 255, 971-975] up to residue 38 and a comparative peptide fingerprint are reported. No obvious homology with the sequences of alpha, pi and mu classes of mammalian glutathione transferases as well as with those of plant glutathione transferases has been noted. These results suggest that the classification so far adopted for glutathione transferases cannot be extended to the bacterial enzyme.
已报道了从奇异变形杆菌中纯化得到的谷胱甘肽转移酶Pm-GST-6.0的N端氨基酸序列（直至第38位残基）以及一个比较肽指纹图谱。未发现其与哺乳动物谷胱甘肽转移酶α、π和μ类的序列以及植物谷胱甘肽转移酶的序列有明显同源性。这些结果表明，目前采用的谷胱甘肽转移酶分类方法不能推广到细菌酶。
