Andreas Humm

TL;DR: The polypeptide fold of NAP and the arrangement of the cofactors is related to that of Escherichia coli formate dehydrogenase (FDH) and distantly resembles dimethylsulphoxide reductase.

TL;DR: The production of telluromethionine-proteins as heavy-atom derivatives offers a valid and general approach in X-ray analysis by the method of multiple isomorphous replacement.

TL;DR: The crystal structure of the recombinant human enzyme by multiple isomorphous replacement at 1.9 Å resolution is determined and a reaction mechanism with a catalytic triad Cys–His–Asp is proposed on the basis of substrate and product bound states.

TL;DR: Molecular modeling revealed a possible binding mode for the second substrate scyllo-inosamine 4-phosphate and the residues which are involved in substrate binding and catalysis are conserved in AT and StrB1 and are at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.

TL;DR: A new method for the removal of N-terminal fusion peptides by means of an immobilized snake venom prothrombin activator is established and cysteine-407 is identified as the active-site residue of AT by radioactive labelling and isolation of labelled peptides, and by site-directed mutagenesis of the protein.