Prediction of secondary structure by evolutionary comparison: Application to the α subunit of tryptophan synthase

1987 ◽  
Vol 2 (2) ◽  
pp. 118-129 ◽  
Author(s):  
Irving P. Crawford ◽  
Thomas Niermann ◽  
Kasper Kirschner
Keyword(s):  
Secondary Structure ◽  
Tryptophan Synthase ◽  
Α Subunit ◽  
Evolutionary Comparison ◽  
Prediction Of Secondary Structure

Study and Prediction of Secondary Structure for Membrane Proteins

2007 ◽  
Vol 24 (4) ◽  
pp. 421-427 ◽  
Author(s):  
Svetlana R. Amirova ◽  
Juri V. Milchevsky ◽  
Ivan V. Filatov ◽  
Natalia G. Esipova ◽  
Vladimir G. Tumanyan
Keyword(s):  
Secondary Structure ◽  
Membrane Proteins ◽  
Prediction Of Secondary Structure

scholarly journals Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile,Pyrococcus furiosus

2000 ◽  
Vol 276 (14) ◽  
pp. 11062-11071 ◽  
Author(s):  
Yuriko Yamagata ◽  
Kyoko Ogasahara ◽  
Yusaku Hioki ◽  
Soo Jae Lee ◽  
Atsushi Nakagawa ◽  
...  
Keyword(s):  
Pyrococcus Furiosus ◽  
Tryptophan Synthase ◽  
Α Subunit ◽  
Entropic Stabilization

scholarly journals Directed evolution of the tryptophan synthase β-subunit for stand-alone function recapitulates allosteric activation

2015 ◽  
Vol 112 (47) ◽  
pp. 14599-14604 ◽  
Author(s):  
Andrew R. Buller ◽  
Sabine Brinkmann-Chen ◽  
David K. Romney ◽  
Michael Herger ◽  
Javier Murciano-Calles ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Pyrococcus Furiosus ◽  
Tryptophan Synthase ◽  
Β Subunit ◽  
Allosteric Activation ◽  
Α Subunit ◽  
X Ray ◽  
Catalytic Activities ◽  
Catalytic Potential ◽  
Protein Partners

Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the β-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native αββα complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the α-subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the α-subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope.

Characterization of a slow folding reaction for the α subunit of tryptophan synthase

1987 ◽  
Vol 2 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Mark R. Hurle ◽  
Greg A. Michelotti ◽  
Mark M. Crisanti ◽  
C. Robert Matthews
Keyword(s):  
Tryptophan Synthase ◽  
Α Subunit
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