Effects of Monovalent Cations on Functional Properties of the Tryptophan Synthase α2β2 Complex in Solution and in the Crystal
作者： A. Peracchi , A. Mozzarelli , G. L. Rossi
DOI: 10.1007/978-3-0348-7393-2_20
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摘要: Synthesis of L-tryptophan, catalyzed by tryptophan synthase from Salmonella typhimurium, at 10°C is activated monovalent cations in the order Cs+ > Rb+ Li+ K+ Na+. The most efficient increase Vmax and decrease KM for indole, Na+ only affects KM. In absence equilibrium distribution external aldimine α-aminoacrylate Schiff base depends on both solution crystalline state. least activating ions, K+, stabilize aldimine, whereas Cs+, favor accumulation a species absorbing 470 nm, tentatively identified as tautomer α-aminoacrylate. Activation enzyme might be associated with stabilization this more reactive intermediate.
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sci-hub.st 参考文章(20)
Charles Yanofsky, Irving P. Crawford, 1 Tryptophan Synthetase The Enzymes. ,vol. 7, pp. 1- 31 ,(1972) , 10.1016/S1874-6047(08)60445-X
Edith Wilson Miles, Hidehiko Kumagai, Modification of Essential Histidyl Residues of the β2 Subunit of Tryptophan Synthetase by Photo-oxidation in the Presence of Pyridoxal 5'-Phosphate and l-Serine and by Diethylpyrocarbonate Journal of Biological Chemistry. ,vol. 249, pp. 2843- 2851 ,(1974) , 10.1016/S0021-9258(19)42707-5
Edith Wilson Miles, Structural Basis for Catalysis by Tryptophan Synthase Advances in Enzymology - and Related Areas of Molecular Biology. ,vol. 64, pp. 93- 172 ,(1991) , 10.1002/9780470123102.CH3
H Kawasaki, R Bauerle, G Zon, S A Ahmed, E W Miles, Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits. Journal of Biological Chemistry. ,vol. 262, pp. 10678- 10683 ,(1987) , 10.1016/S0021-9258(18)61017-8
Edith Wilson Miles, Tryptophan Synthase: Structure, Function, and Subunit Interaction Advances in Enzymology - and Related Areas of Molecular Biology. ,vol. 49, pp. 127- 186 ,(1979) , 10.1002/9780470122945.CH4
X.J. Yang, E.W. Miles, Threonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex. Journal of Biological Chemistry. ,vol. 267, pp. 7520- 7528 ,(1992) , 10.1016/S0021-9258(18)42548-3
A Mozzarelli, A Peracchi, G L Rossi, S A Ahmed, E W Miles, Microspectrophotometric studies on single crystals of the tryptophan synthase alpha 2 beta 2 complex demonstrate formation of enzyme-substrate intermediates. Journal of Biological Chemistry. ,vol. 264, pp. 15774- 15780 ,(1989) , 10.1016/S0021-9258(18)71544-5
S A Ahmed, E W Miles, D R Davies, Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium. Journal of Biological Chemistry. ,vol. 260, pp. 3716- 3718 ,(1985) , 10.1016/S0021-9258(19)83682-7
C C Hyde, S A Ahmed, E A Padlan, E W Miles, D R Davies, Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. Journal of Biological Chemistry. ,vol. 263, pp. 17857- 17871 ,(1988) , 10.1016/S0021-9258(19)77913-7
Paul F. Cook, Shinichi Hara, Srinivasa Nalabolu, Klaus D. Schnackerz, pH Dependence of the absorbance and phosphorus-31 NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine Biochemistry. ,vol. 31, pp. 2298- 2303 ,(1992) , 10.1021/BI00123A013