|Related Categories||4.2.x.x C-O bonds, 4.x.x.x Lyases, Biochemicals and Reagents, Enzyme Class Index, Enzymes, Inhibitors, and Substrates More...|
Currently available only in Europe.
Bottomless glass bottle. Contents are inside inserted fused cone.
1 Trp-U corresponds to the amount of enzyme which produces 0.1 μmol of tryptophan in 20 minutes at pH 7.8 and 37 °C.
Tryptophan synthase is an α2β2 enzyme that catalyzes the final two steps in the biosynthesis of L-tryptophan. It is used to study tryptophan inhibitors to treat various diseases, to study the plasticity of the tryptophase synthase active site and to study allosteric communication 1. Product 96159 produces tryptophan at pH 7.8 and 37 °C.
The α subunit cleaves indole-3-glycerol phosphate into indole and glyceraldehyde 3-phosphate. Indole is then channeled to the active site of the β-subunit and condensed with PLP-bound α-aminoacrylate. Tryptophan synthase is allosterically regulated 1.
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Patients with Chlamydia-associated arthritis have ocular (trachoma), not genital, serovars of C. trachomatis in synovial tissue. Gerard HC, Stanich JA, Whittum-Hudson JA, et al. Microb. Pathog. 48(2), 62-8, (2010)
Effects of hydrostatic pressure on the conformational equilibrium of tryptophan synthase from Salmonella typhimurium. Phillips RS, Miles EW, McPhie P, et al. Ann. N. Y. Acad. Sci. 1189, 95-103, (2010)
Activation of camalexin biosynthesis in Arabidopsis thaliana in response to perception of bacterial lipopolysaccharides: a gene-to-metabolite study. Beets CA, Huang JC, Madala NE, et al. Planta 236(1), 261-72, (2012)
The most stable protein-ligand complex: applications for one-step affinity purification and identification of protein assemblies. Giese C, Zosel F, Puorger C, et al. Angew. Chem. Int. Ed. Engl. 51(18), 4474-8, (2012)
Directed evolution of (βα)(8)-barrel enzymes: establishing phosphoribosylanthranilate isomerisation activity on the scaffold of the tryptophan synthase α-subunit. Evran S, Telefoncu A, and Sterner R Protein Eng. Des. Sel. 25(6), 285-93, (2012)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?