Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites

Biochemistry ◽  
1983 ◽  
Vol 22 (7) ◽  
pp. 1650-1656 ◽  
Author(s):  
Richard I. Christopherson ◽  
Elizabeth Heyde ◽  
John F. Morrison

2005 ◽  
Vol 71 (11) ◽  
pp. 7224-7228 ◽  
Author(s):  
Tina Lütke-Eversloh ◽  
Gregory Stephanopoulos

ABSTRACT In order to get insights into the feedback regulation by tyrosine of the Escherichia coli chorismate mutase/prephenate dehydrogenase (CM/PDH), which is encoded by the tyrA gene, feedback-inhibition-resistant (fbr) mutants were generated by error-prone PCR. The tyrA fbr mutants were selected by virtue of their resistance toward m-fluoro-d,l-tyrosine, and seven representatives were characterized on the biochemical as well as on the molecular level. The PDH activities of the purified His6-tagged TyrA proteins exhibited up to 35% of the enzyme activity of TyrAWT, but tyrosine did not inhibit the mutant PDH activities. On the other hand, CM activities of the TyrAfbr mutants were similar to those of the TyrAWT protein. Analyses of the DNA sequences of the tyrA genes revealed that tyrA fbr contained amino acid substitutions either at Tyr263 or at residues 354 to 357, indicating that these two sites are involved in the feedback inhibition by tyrosine.



Biochemistry ◽  
1991 ◽  
Vol 30 (31) ◽  
pp. 7777-7782 ◽  
Author(s):  
Joanne Turnbull ◽  
W. W. Cleland ◽  
John F. Morrison


1982 ◽  
Vol 717 (1) ◽  
pp. 6-11 ◽  
Author(s):  
Suresh B. Bhosale ◽  
Julian I. Rood ◽  
Margaret K. Sneddon ◽  
John F. Morrison






Biochemistry ◽  
1977 ◽  
Vol 16 (10) ◽  
pp. 2312-2312
Author(s):  
Cheng-Wen Wu ◽  
Lynwood Yarbrough ◽  
Felicia Wu ◽  
Zaharia Hillel


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