Way station. Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5′-phosphate (PLP)-dependent enzymes. Whereas structures of other PLP-bound reaction intermediates have been determined, a high-quality structure of a quinonoid species has not been reported. We present the crystal structure of the indoline quinonoid intermediate of tryptophan synthase (see figure) and discuss its implications for the enzymatic mechanism and allosteric regulation
In the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the alpha-site...
Pyridoxal-5’-Phosphate (PLP) enzymes are essential cofactors in many important enzymatic mechanisms....
We determined the 2.25 Å resolution crystal structure of the βA169L/βC170W mutant form of the trypto...
Way station. Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5′-phos...
Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5'-phosphate-depende...
Chemical−level details such as protonation and hybridization state are critical for understanding en...
Chemical−level details such as protonation and hybridization state are critical for understanding en...
Tryptophan synthase is a pyridoxal 5'-phosphate-dependent alpha(2)beta(2) complex catalyzing the las...
Tryptophan synthase (TrpS) is a pyridoxal phosphate-containing bifunctional enzyme that catalyzes th...
Carbanionic intermediates play a central role in the catalytic transformations of amino acids perfor...
The binding of substrates and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and t...
Crystal structures of wild-type tryptophan synthase α2β2 complexes from Salmonella typhim...
We used freeze trapping to stabilize the Michaelis complex of wild-type tryptophan synthase and the ...
Abstract Microspectrophotometry of single crystals of the tryptophan synthase alpha 2 beta 2 complex...
Protonation and hybridization state are critical phenomena at the chemical-level that are vital in u...
In the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the alpha-site...
Pyridoxal-5’-Phosphate (PLP) enzymes are essential cofactors in many important enzymatic mechanisms....
We determined the 2.25 Å resolution crystal structure of the βA169L/βC170W mutant form of the trypto...
Way station. Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5′-phos...
Quinonoid intermediates play a key role in the catalytic mechanism of pyridoxal 5'-phosphate-depende...
Chemical−level details such as protonation and hybridization state are critical for understanding en...
Chemical−level details such as protonation and hybridization state are critical for understanding en...
Tryptophan synthase is a pyridoxal 5'-phosphate-dependent alpha(2)beta(2) complex catalyzing the las...
Tryptophan synthase (TrpS) is a pyridoxal phosphate-containing bifunctional enzyme that catalyzes th...
Carbanionic intermediates play a central role in the catalytic transformations of amino acids perfor...
The binding of substrates and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and t...
Crystal structures of wild-type tryptophan synthase α2β2 complexes from Salmonella typhim...
We used freeze trapping to stabilize the Michaelis complex of wild-type tryptophan synthase and the ...
Abstract Microspectrophotometry of single crystals of the tryptophan synthase alpha 2 beta 2 complex...
Protonation and hybridization state are critical phenomena at the chemical-level that are vital in u...
In the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the alpha-site...
Pyridoxal-5’-Phosphate (PLP) enzymes are essential cofactors in many important enzymatic mechanisms....
We determined the 2.25 Å resolution crystal structure of the βA169L/βC170W mutant form of the trypto...