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A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC

Publications associées (53)

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Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or Hofmeister series of cations and anions. Since its first formulation in 1888, this series has been invoked in a plethora of effects, going beyond the original ...

Amer Chemical Soc2017

Structure of a pathogen effector reveals the enzymatic mechanism of a novel acetyltransferase family

Shuguang Yuan

Effectors secreted by the type Ill secretion system are essential for bacterial pathogenesis. Members of the Yersinia outer-protein J (YopJ) family of effectors found in diverse plant and animal pathogens depend on a protease-like catalytic triad to acetyl ...

Nature Publishing Group2016

Alkaline phosphatase-fused repebody as a new format of immuno-reagent for an immunoassay

Oliver Hantschel

Enzyme-linked immunoassays based on an antibody-antigen interaction are widely used in biological and medical sciences. However, the conjugation of an enzyme to antibodies needs an additional chemical process, usually resulting in randomly cross-linked mol ...

Elsevier2016

Establishing the Catalytic Mechanism of Human Pancreatic α-Amylase with QM/MM Methods

Marta Andreia Da Silva Perez

In this work, we studied the catalytic mechanism of human pancreatic α-amylase (HPA). Our goal was to determine the catalytic mechanism of HPA with atomic detail using computational methods. We demonstrated that the HPA catalytic mechanism consists of two ...

2015

Reaction Mechanism and Catalytic Fingerprint of Allantoin Racemase

Matteo Dal Peraro, Marco Stenta, Thomas Lemmin, Matteo Thomas Degiacomi, Christophe Bovigny

The stereospecific oxidative decomposition of urate into allantoin is the core of purine catabolism in many organisms. The spontaneous decomposition of upstream intermediates and the nonenzymatic racemization of allantoin lead to an accumulation of (R)-all ...

Amer Chemical Soc2014

B-12-dependent enzymes employ radical species with exceptional prowess to catalyze some of the most chemically challenging, thermodynamically unfavorable reactions. However, dealing with highly reactive intermediates is an extremely demanding task, requiri ...

2014

[Fe]-hydrogenase is a newly characterized type of hydrogenase. This enzyme heterolytically splits hydrogen in the presence of a natural substrate. The active site of the enzyme contains a mono-iron complex with intriguing ironacyl ligation. Several groups ...

Wiley-V C H Verlag Gmbh2013

Geometry as a Catalyst: How Vapor Cavities Nucleate from Defects

Simone Meloni

The onset of cavitation is strongly enhanced by the presence of rough surfaces or impurities in the liquid. Despite decades of research, the way the geometry of these defects promote the nucleation of bubbles and its effect on the kinetics of the process r ...

Amer Chemical Soc2013

Role of Environment for Catalysis of the DNA Repair Enzyme MutY

Ursula Röthlisberger, Jeremy Samuel Arey, Elizabeth Claire Brunk

Control of the N-glycosylase reaction by the DNA repair enzyme, MutY, entails the organization of solvent molecules. Classical molecular dynamics and QM/MM simulations were used to investigate the solvent and environment effects contributing to catalysis. ...

2012

On the active site of mononuclear B1 metallo beta-lactamases: a computational study

Matteo Dal Peraro, Paolo Carloni

Metallo-beta-lactamases (M beta Ls) are Zn(II)-based bacterial enzymes that hydrolyze beta-lactam antibiotics, hampering their beneficial effects. In the most relevant subclass (B1), X-ray crystallography studies on the enzyme from point to either two zinc ...

2012