The role of the extra helix α0 in the N-terminal extension of the eight-fold βα barrel of
indoleglycerol phosphate synthase was probed by point mutation and truncation. Replacing …

Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in the biosynthesis of
tryptophan. It belongs to the large and versatile family of (βα) 8-barrel enzymes but has an …

The stability and activity of indole-3-glycerol phosphate synthase from Sulfolobus
solfataricus were studied as a function of pH and temperature. In this paper we focus on …

As a test of the hypothesis that folding mechanisms are better conserved than sequences in
TIM barrels, the equilibrium and kinetic folding mechanisms of indole-3-glycerol phosphate …

To test the roles of motif and amino acid sequence in the folding mechanisms of TIM barrel
proteins, hydrogen-deuterium exchange was used to explore the structure of the stable …

Abstract Indole-3-glycerol-phosphate synthase, a thermophilic and thermostable enzyme
from the archaeon Sulfolobus solfataricus, was purified and characterized. The sequence of …

The recombinantly expressed protein indoleglycerol phosphate synthase from the
hyperthermophilic bacterium Thermotoga maritima (tIGPS) was purified and characterized …

Indoleglycerol phosphate synthase catalyzes the ring closure of 1‐(2‐carboxyphenylamino)‐
1‐deoxyribulose 5′‐phosphate to indoleglycerol phosphate, the fifth step in the pathway of …

The crystal structure of the thermostable indoleglycerol-phosphate synthase from
Thermotoga maritima (tIGPS) was determined at 2.5 Å resolution. It was compared with the …

It is important to understand how the catalytic activity of enzymes is related to their
conformational flexibility. We have studied this activity–flexibility correlation using the …