Title |
Inhibitors of 3-Deoxy-Darabino-heptulosonate-7-phosphate Synthetase from Streptomyces caespitosus |
Author |
Yoo, Jin-Cheol * · Kim, Sung-Jung¹ · Lee, Jung-Jun² |
Address |
Department of Pharmacy; ¹Department of Genetic Engineering, Chosun University; ²Genetic Enginneering Research Institute, KIST |
Bibliography |
Korean Journal of Microbiology, 31(6),550-554, 1993 |
DOI |
|
Key Words |
Streptomyces caespitosus, DAHP synthetase, regulation |
Abstract |
3-Deoxy-Darabino-heptulosonate-7-phosphate(DAHP) synthetast, the first enzyme of the shikimate pathway was strongly inhibited by L-tryptophan. This enzyme ws inhibited weakly by shikimate and rifamycin SV but was not inhibited by mitomycin C which isbiosynthesized from Streptomyces caespitosus. Inhibition by tryptophan was not competitive with respect to phosphoenolpyruvate(PEP) and D-erythrose-4-phosphate(E-4-P) but was influenced by the presence of Co^2+. The enzyme activity was inhibited by excess of E-4-P added in the enzyme assay system. D-Xylulose-5-phosphate(X-5-P), D-fructose-6-phosphate(F-6-p), D-ribose-5-phosphate(R-5-P) or D-glucose-6-Phosphate(G-6-P) inhibited DAHP synthtase in cell free extract, but no inhibitory effects were detected on partially pruified enzyme or purified enzyme. It appears that the indirect inhibition of sugar phosphates was considered to be due to the formation of E-4-P generated by the related enzymes in zymes in curde cell extract. |
Download PDF |
Kor_310614_550-554p.pdf |