Günter Auerbach

TL;DR: Based on gene cloning, recombinant expression, mutagenesis studies, structural analysis of crystals and NMR studies, reaction mechanisms for the biosynthetic and recycling enzymes were proposed, and BH(4) deficiency due to autosomal recessive mutations in all enzymes (except sepiapterin reductase) have been described as a cause of hyperphenylalaninaemia.

TL;DR: Structural analysis of TmLDH and comparison of the enzyme to moderately thermophilic and mesophilic homologs reveals a strong conservation of both the three-dimensional fold and the catalytic mechanism.

TL;DR: The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model to contain an essential zinc ion coordinated to a His side chain.

TL;DR: GTP cyclohydrolase I of Escherichia coli is a torus-shaped homodecamer with D5 symmetry and catalyzes a complex ring expansion reaction conducive to the formation of dihydroneopterin triphosphate from GTP.

TL;DR: The crystal structure of PGK from the hyperthermophilic organism Thermotoga maritima represents the first structure of an extremely thermostable PGK and provides new details of the catalytic mechanism, including the hinge-bending motion of the two domains upon closure of the structure.