Crystallization and partial characterization of dimethylallyl pyrophosphate: L-tryptophan dimethylallyltransferase from Claviceps sp. SD58.
作者： W.A. Cress , L.T. Chayet , H.C. Rilling
DOI: 10.1016/S0021-9258(19)68532-7
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摘要: Dimethylallyl pyrophosphate: L-tryptophan dimethylallyltransferase (dimethylallyl tryptophan synthetase) has been purified from Claviceps strain SD58 to a homogeneous crystalline form. The enzyme is pure as judged by polyacrylamide gel electrophoresis and contains two similar subunits of 34,000 molecular weight shown in gels containing sodium dodecyl sulfate. Since the was determined have 70,000 exclusion chromatography, it dimeric. substrates dimethylallyl pyrophosphate each mixed (negative positive) cooperativity with minimum Hill coefficient 0.37 0.73, respectively. Calcium ion positive allosteric effector and, at 20 mM concentration, deregulates enzyme. deregulated Km values 7.2 microM for 8.8 tryptophan. Vmax under conditions 953 nmol/min/mg, giving turnover number 14. Ca2+ S[0.5] 4.5 mM. kinetic mechanism random sequential.
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