scispace - formally typeset
N

Nicholas Schramek

Researcher at Technische Universität München

Publications -  38
Citations -  1416

Nicholas Schramek is an academic researcher from Technische Universität München. The author has contributed to research in topics: GTP' & GTP cyclohydrolase I. The author has an hindex of 23, co-authored 38 publications receiving 1332 citations.

Papers
More filters
Journal ArticleDOI

Artemisinin biosynthesis in growing plants of Artemisia annua. A 13CO2 study.

TL;DR: The isotopologue data confirm the previously proposed mechanisms for the cyclization of (E,E)-FPP to amorphadiene and its oxidative conversion to artemisinin and support deprotonation of a terminal allyl cation intermediate as the final step in the enzymatic conversion of FPP to amorpha-4,11-diene.
Journal ArticleDOI

IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis.

TL;DR: The implementation of a gene cassette directing the overexpression of the isc operon involved in the assembly of iron-sulfur clusters into an Escherichia coli strain engineered for ispH gene expression increased the catalytic activity of IspH protein anaerobically purified from this strain by a factor of at least 200.
Journal ArticleDOI

Biosynthesis of terpenoids: 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase from tomato.

TL;DR: The putative catalytic domain of a predicted tomato protein with similarity to 4-diphosphocytidyl-2-C-methyl-d-erythritol kinase of Escherichia coli was expressed in a recombinant E. coli strain and was shown to catalyze the phosphorylation of the position 2 hydroxy group.
Journal ArticleDOI

Biosynthesis of Pteridines NMR STUDIES ON THE REACTION MECHANISMS OF GTP CYCLOHYDROLASE I, PYRUVOYLTETRAHYDROPTERIN SYNTHASE, AND SEPIAPTERIN REDUCTASE

TL;DR: Multinuclear NMR experiments showed that the reaction catalyzed by GTP cyclohydrolase I involves the release of a proton from C-2′ of GTP that is exchanged with the bulk solvent that is reintroduced stereospecifically from the Bulk solvent.
Journal ArticleDOI

Biosynthesis of Pteridines. Reaction Mechanism of GTP Cyclohydrolase I

TL;DR: Comparison between the wild-type and mutant enzyme structures indicates that the catalytically active zinc ion is directly coordinated to Cys110, Cys181 and His113, as well as to a water molecule, which is in close hydrogen bond contact to His112.