122 

 must encode an intact bifunctional S-protein. On the 

 other hand, SPIO and SP33 trans formants would not grow on M9 

 medium unless aromatic amino acids were supplied. Table 7- 

 1 shows results obtained by direct enzyme assays of 

 transformants carrying an aroD»aroE insert, in comparison to 

 appropriate controls. These data show that expression 

 levels of both DQT and SDH are about 15 -fold higher than the 

 wild type E. coli levels which have the corresponding 

 activities. 



Table 7-1. SDH/DQT activities in transformed aroD 

 and aroE mutant strains of E. coli. 



Specific Activities 

 Enzyme 



Preparation DQT SDH 



aroD AT1360 1.3 



aroD AT1360 (+SP3) 15.0 18.7 



aroE Sk4 94 0.7 



aroE SK4 94 (+SP3) 11.4 17.9 



Initial sequence analysis of cDNA clones 



Analysis of the sequenced 5' and 3' ends of the 5 

 possible SP-clones, by the GCG Blast computer program, 

 revealed that one clone, SPIO was NADP^-specif ic malate 

 dehydrogenase and that SP33 was NADP*- specif ic cinnamyl- 

 alcohol dehydrogenase (about 100% identity) . The three 

 remaining clones, SP3 , SP5, and SP6 were identical. The 5' 



