The field of bioinorganic chemistry is at a propitious stage of development. Ever more
complex metallobiomolecules are isolated and purified, physical methodologies and …

▪ Abstract Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic
groups that are required to sustain fundamental life processes. Owing to their remarkable …

The focus of this review is the human de novo purine biosynthetic pathway. The pathway
enzymes are enumerated, as well as the reactions they catalyze and their physical …

Interactions among the residues in the serine protease Asp-His–Ser catalytic triad, in the
special environment of the enzyme–substrate complex, activate the nucleophilic potential of …

The catalytic action of serine peptidases depends on the interplay of a nucleophile, a
general base and an acid. In the classic trypsin and subtilisin families this catalytic triad is …

THE crystal structures of three amidohydrolases have been determined recently1–3:
glutamine PRPP amidotransferase (GAT), penicillin acylase, and the proteasome. These …

The nitrilase superfamily consists of thiol enzymes involved in natural product biosynthesis
and post-translational modification in plants, animals, fungi and certain prokaryotes. On the …

▪ Abstract The three-dimensional structures of tryptophan synthase, carbamoyl phosphate
synthetase, glutamine phosphoribosylpyrophosphate amidotransferase, and asparagine …

The 3‐D structure of Bacillus cereus (569/H/9) beta‐lactamase (EC 3.5. 2.6), which
catalyses the hydrolysis of nearly all beta‐lactams, has been solved at 2.5 A resolution by …

▪ Abstract Proteasomes are large multisubunit proteases that are found in the cytosol, both
free and attached to the endoplasmic reticulum, and in the nucleus of eukaryotic cells. Their …