Bonner C A, Jensen R A
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611-0100.
Biochem J. 1994 Aug 15;302 ( Pt 1)(Pt 1):11-4. doi: 10.1042/bj3020011.
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues.
克隆并测序了编码具有脱氢奎宁酶和莽草酸脱氢酶催化结构域的双功能蛋白的烟草cDNA。成功地对大肠杆菌aroD和aroE营养缺陷型进行了互补。氨基酸测序确定了成熟蛋白的N端。与原核生物同源物相比,这两个催化结构域与酵母和真菌同源物的氨基酸同一性更高。