Imidazole glycerol phosphate synthase (HisFH) is a heterodimeric bienzyme complex
operating at a central branch point of metabolism. HisFH is responsible for the HisH …

To better understand the evolution of a key metabolic pathway, we have sequenced the
trpCFBA gene cluster of the hyperthermophilic bacterium Thermotoga maritima. The genes …

Publisher Summary This chapter discusses the folding pathway of triosephosphate
isomerase (TIM), which is a widely studied enzyme. The ubiquity, efficient catalytic activity …

The urea-induced equilibrium unfolding of the α-subunit of tryptophan synthase (αTS) from
Escherichia coli can be described by a four-state model, N⇌ I1⇌ I2⇌ U, involving two highly …

As for many enzymes, the enzymatic pathway of triosephosphate isomerase (TIM) includes
the partially rate determining motion of an active site loop (loop 6, residues 166− 176), which …

Pyridoxal 5 '-phosphate (PLP) is the biologically active form of vitamin B6 and is an
important cofactor for several of the enzymes involved in the metabolism of amine …

HisF (imidazole glycerol phosphate synthase) is an important branch-point enzyme in the
histidine biosynthetic pathway of microorganisms. Because of its potential relevance for …

A possible approach to generate enzymes with an engineered temperature optimum is to
create chimeras of homologous enzymes with different temperature optima. We tested this …

Protein evolution proceeds by a complex response of organismal fitness to mutations that
can simultaneously affect protein stability, structure, and enzymatic activity. To probe the …

In previous work we tested what three amino acid sequences could serve as a protein hinge
in triosephosphate isomerase [Sun, J., and Sampson, NS (1998) Protein Sci. 7, 1495 …