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Erratum: The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography

Georg Wille
Danilo Meyer
Kai Tittmann
Amendments and Corrections01 Jul 2006
Nature Chemical Biology

Volume: 2, P: 390
Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates

Plant-specific class III glutaredoxins regulate the activity of TGA transcription factors. Here, the authors show that that ROXY9, a member of the class III of glutaredoxins, lacks oxidoreductase activity due to unfavourable positioning of glutathione. Consequently, class III glutaredoxins may not regulate gene expression through redox modifications of target proteins.

Pascal Mrozek
Stephan Grunewald
Christiane Gatz
ResearchOpen Access11 Jan 2025
Nature Communications

Volume: 16, P: 1-15
Observation of a stable carbene at the active site of a thiamin enzyme

Carbenes have been postulated to take part in the catalytic cycle of several enzymes, but direct detection of these unstable compounds has been elusive. Spectroscopic and structural studies of pyruvate oxidase now identify a carbene-containing cofactor, calling for reinspection of existing enzyme mechanisms.

Danilo Meyer
Piotr Neumann
Kai Tittmann
Research09 Jun 2013
Nature Chemical Biology

Volume: 9, P: 488-490
The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography

Georg Wille
Danilo Meyer
Kai Tittmann
Research07 May 2006
Nature Chemical Biology

Volume: 2, P: 324-328
Transformers at the interface

Recent studies on two enzyme classes operating at the membrane interface showcase an unanticipated degree of structural plasticity involving domain swapping and marked secondary structure reshuffling. This structural variability in topology is key to functional diversification and catalytic prowess.

Florian Brodhun
Kai Tittmann
News & Views12 Jan 2015
Nature Chemical Biology

Volume: 11, P: 102-103
Multiple redox switches of the SARS-CoV-2 main protease in vitro provide opportunities for drug design

Here the authors demonstrate that the SARS-CoV-2 main protease (Mpro) is subject to redox regulation in vitro, reversibly switching between the enzymatically active dimer and the functionally dormant monomer through redox modifications of cysteine residues.

Lisa-Marie Funk
Gereon Poschmann
Kai Tittmann
ResearchOpen Access09 Jan 2024
Nature Communications

Volume: 15, P: 1-18
A lysine–cysteine redox switch with an NOS bridge regulates enzyme function

A NOS bridge between cysteine and lysine residues serves as an allosteric redox switch in the transaldolase enzyme of Neisseria gonorrhoeae, demonstrating the existence of protein regulatory switches that contain covalent crosslinks other than disulfides.

Marie Wensien
Fabian Rabe von Pappenheim
Kai Tittmann
Research05 May 2021
Nature

Volume: 593, P: 460-464
Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis

Ground state destabilization is often evoked as a possible explanation of orotidine-5′-phosphate decarboxylase catalysis. Now, high-resolution structures of this enzyme provide time-resolved snapshots along its reaction coordinate revealing that transition-state stabilization by electrostatic interactions drives its reactivity.

Sören Rindfleisch
Matthias Krull
Kai Tittmann
Research21 Apr 2022
Nature Catalysis

Volume: 5, P: 332-341
Widespread occurrence of covalent lysine–cysteine redox switches in proteins

A survey of protein structures identifies widespread lysine–cysteine cross-links in functionally diverse proteins across all domains of life and in various structural motifs, where these redox switches control enzyme catalysis and/or ligand binding.

Fabian Rabe von Pappenheim
Marie Wensien
Kai Tittmann
ResearchOpen Access14 Feb 2022
Nature Chemical Biology

Volume: 18, P: 368-375
Structural basis for antibiotic action of the B₁ antivitamin 2′-methoxy-thiamine

Structural and biochemical analysis of E. coli transketolase with 2′-methoxy-thiamine shows that this antivitamin selectively inhibits the bacterial enzyme via a steric clash with a critical glutamate residue, preventing cofactor activation.

Fabian Rabe von Pappenheim
Matteo Aldeghi
Kai Tittmann
Research24 Aug 2020
Nature Chemical Biology

Volume: 16, P: 1237-1245
Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate

Structural analysis of the enzyme transketolase at sub-ångström resolution shows the existence of physically distorted covalent intermediates with elongated scissile substrate bonds. These observations highlight the ability of enzymes to enhance the reactivity of reaction intermediates leading to a more efficient process.

Stefan Lüdtke
Piotr Neumann
Kai Tittmann
Research18 Aug 2013
Nature Chemistry

Volume: 5, P: 762-767
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes

Alexander Kaplun
Elad Binshtein
Boaz Shaanan
Research06 Jan 2008
Nature Chemical Biology

Volume: 4, P: 113-118
Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism

The first high-resolution structures of transaldolase with bound intermediates both define active site residues that necessitate a revision of the current reaction pathway and point to a high-energy intermediate structure and protein conformational changes as mechanisms to promote product formation.

Anja Lehwess-Litzmann
Piotr Neumann
Kai Tittmann
Research21 Aug 2011
Nature Chemical Biology

Volume: 7, P: 678-684
ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space

ProteoPlex optimizes buffer conditions for the isolation and purification of macromolecular complexes. The concurrent complex stabilization is beneficial for structure determination using X-ray crystallography or cryo-electron microscopy.

Ashwin Chari
David Haselbach
Holger Stark
Research03 Aug 2015
Nature Methods

Volume: 12, P: 859-865
Low-barrier hydrogen bonds in enzyme cooperativity

Structural and biophysical studies reveal that low-barrier hydrogen bonds enable long-range communication between the active sites of multimeric enzymes and synchronise catalysis.

Shaobo Dai
Lisa-Marie Funk
Kai Tittmann
Research18 Sept 2019
Nature

Volume: 573, P: 609-613
Genetic correlation between amyotrophic lateral sclerosis and schizophrenia

Relatives of patients with amyotrophic lateral sclerosis have an unexpectedly high incidence of schizophrenia. Here, the authors show a genetic link between the two conditions, suggesting shared neurobiological mechanisms.

Russell L. McLaughlin
Dick Schijven
Michael C. O’Donovan
ResearchOpen Access21 Mar 2017
Nature Communications

Volume: 8, P: 1-12
Structural Analysis of an Evolved Transketolase Reveals Divergent Binding Modes

Pierre E. Affaticati
Shao-Bo Dai
Paul A. Dalby
ResearchOpen Access21 Oct 2016
Scientific Reports

Volume: 6, P: 1-10

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