Allosteric Interactions Coordinate Catalytic Activity between Successive Metabolic Enzymes in the Tryptophan Synthase Bienzyme Complex

Peter S. Brzovic; Khiet Ngo; Michael F. Dunn

doi:10.1021/bi00130a014

Allosteric Interactions Coordinate Catalytic Activity between Successive Metabolic Enzymes in the Tryptophan Synthase Bienzyme Complex

Peter S. Brzovic, Khiet Ngo, Michael F. Dunn

Research output: Contribution to journal › Article › peer-review

Original language	English
Pages (from-to)	3831-3839
Number of pages	9
Journal	Biochemistry
Volume	31
Issue number	15
DOIs	https://doi.org/10.1021/bi00130a014
State	Published - Apr 1 1992
Externally published	Yes

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Biochemistry

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title = "Allosteric Interactions Coordinate Catalytic Activity between Successive Metabolic Enzymes in the Tryptophan Synthase Bienzyme Complex",

author = "Brzovic, {Peter S.} and Khiet Ngo and Dunn, {Michael F.}",

note = "Tryptophan synthase from enteric bacteria is an α 2β 2 bienzyme complex that catalyzes the final two reactions in the biosynthesis of L-tryptophan (L-Trp) from 3-indole-D-glycerol 3′-phosphate (IGP) and L-serine (L-Ser). The bienzyme complex exhibits reciprocal ligand-mediated allosteric interactions between the heterologous subunits [Houben, K., Dunn, M. F.",

year = "1992",

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AU - Ngo, Khiet

AU - Dunn, Michael F.

N1 - Tryptophan synthase from enteric bacteria is an α 2β 2 bienzyme complex that catalyzes the final two reactions in the biosynthesis of L-tryptophan (L-Trp) from 3-indole-D-glycerol 3′-phosphate (IGP) and L-serine (L-Ser). The bienzyme complex exhibits reciprocal ligand-mediated allosteric interactions between the heterologous subunits [Houben, K., Dunn, M. F.

PY - 1992/4/1

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JO - Biochemistry

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Allosteric Interactions Coordinate Catalytic Activity between Successive Metabolic Enzymes in the Tryptophan Synthase Bienzyme Complex

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