Victor Kulik

Synthesis and Characterization of Allosteric Probes of Substrate Channeling in the Tryptophan Synthase Bienzyme Complex (2007)

Ngo, Huu, Harris, Rodney, Kimmich, Novelle, Casino, Patricia, Niks, Dimitri, Blumenstein, Lars, ...

Allosteric interactions regulate substrate channeling in Salmonella typhimurium tryptophan synthase. The channeling of indole between the Alpha− and ß−sites via the interconnecting 25 Å...

Allosteric Regulation of Substrate Channeling in Tryptophan Synthase: Modulation of the L−Serine Reaction in Stage I of the ß−Reaction by Alpha−Site Ligands (2007)

Ngo, H., Kimmich, N., Harris, R., Niks, D., Blumenstein, Lars, Kulik, Victor, ...

n the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the Alpha−site is channeled to the ß−site via a 25 Å long tunnel. Within the ß−site, indole and...

On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase from Salmonella typhimurium and BX1 from Maize, Two Evolutionarily Related Enzymes (2005)

Kulik, Victor, Hartmann, Elisabeth, Weyand, Michael, Frey, Marco, Gierl, Alfons, ...

Indole is a reaction intermediate in at least two biosynthetic pathways in maize seedlings. In the primary metabolism, the α−subunit (TSA) of the bifunctional tryptophan synthase (TRPS) catalyzes...

On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase from Salmonella typhimurium and BX1 from Maize, Two Evolutionarily Related Enzymes (2005)

Kulik, Victor, Hartmann, Elisabeth, Weyand, Michael, Frey, Marco, Gierl, Alfons, ...

Indole is a reaction intermediate in at least two biosynthetic pathways in maize seedlings. In the primary metabolism, the α−subunit (TSA) of the bifunctional tryptophan synthase (TRPS) catalyzes...

On the Role of αThr183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase (2002)

Kulik,Victor, Weyand,Michael, Seidel,Ralf, Niks,Dimitri, Arac,Demet, Dunn,Michael F., ...

The catalytic activity and substrate channeling of the pyridoxal 5-phosphate-dependent tryptophan synthase α 2β 2 complex is regulated by allosteric interactions that modulate the switching of the...

On the role of αThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase (2002)

Kulik,Victor, Weyand,Michael, Seidel,Ralf, Niks,Dimitri, Arac,Demet, Dunn,Michael F., ...

The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching...

On the role of αThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase (2002)

Kulik, Victor, Weyand, Michael, Seidel, Ralf, Niks, Dimitri, Arac, Demet, Dunn, Michael F., ...

The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching...

On the Role of αThr183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase (2002)

Kulik, Victor, Weyand, Michael, Seidel, Ralf, Niks, Dimitri, Arac, Demet, Dunn, Michael F., ...

The catalytic activity and substrate channeling of the pyridoxal 5-phosphate-dependent tryptophan synthase α 2β 2 complex is regulated by allosteric interactions that modulate the switching of the...