Synthesis of azobenzenealkylmaleimide probes to photocontrol the enzyme activity of a bacterial histone deacetylase-like amidohydrolase

Horstmann, Benjamin; Korbus, Michael; Friedmann, Tatjana; Wolff, Christiane; Thiele, Christina M.; Meyer‐Almes, Franz‐Josef

doi:10.1016/j.bioorg.2014.10.004

Cited by 20 publications

(23 citation statements)

References 25 publications

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“…Azobenzene-maleimide probes were attached through a single Cys substitution on an important loop in bacterial histone deacetylase amidohydrolase (HDAH) to create a light-switchable enzyme. 154 The modified HDAH enzyme was more active when the azobenzene photoswitch was in the trans-compared to the cis-configuration, potentially because in the cis-configuration the moiety interacts with the enzyme surface. 155 Surface-exposed Cys residues may in general serve as attachment points for novel, allosteric modulators.…”

Section: Controlling Enzyme Structural Dynamics Through Covalent Consmentioning

confidence: 99%

“…It should be noted that in some cases the azobenzene does not need to act as part of a crosslink to affect an enzyme's catalytic activity. Azobenzene‐maleimide probes were attached through a single Cys substitution on an important loop in bacterial histone deacetylase amidohydrolase (HDAH) to create a light‐switchable enzyme . The modified HDAH enzyme was more active when the azobenzene photoswitch was in the trans ‐ compared to the cis ‐configuration, potentially because in the cis ‐configuration the moiety interacts with the enzyme surface …”

Section: Controlling Enzyme Structural Dynamics Through Covalent Consmentioning

confidence: 99%

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Engineered control of enzyme structural dynamics and function

2018

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Enzymes undergo a range of internal motions from local, active site fluctuations to large-scale, global conformational changes. These motions are often important for enzyme function, including in ligand binding and dissociation and even preparing the active site for chemical catalysis. Protein engineering efforts have been directed towards manipulating enzyme structural dynamics and conformational changes, including targeting specific amino acid interactions and creation of chimeric enzymes with new regulatory functions. Post-translational covalent modification can provide an additional level of enzyme control. These studies have not only provided insights into the functional role of protein motions, but they offer opportunities to create stimulus-responsive enzymes. These enzymes can be engineered to respond to a number of external stimuli, including light, pH, and the presence of novel allosteric modulators. Altogether, the ability to engineer and control enzyme structural dynamics can provide new tools for biotechnology and medicine.

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Section: Controlling Enzyme Structural Dynamics Through Covalent Consmentioning

confidence: 99%

Section: Controlling Enzyme Structural Dynamics Through Covalent Consmentioning

confidence: 99%

Engineered control of enzyme structural dynamics and function

2018

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“…In the last years, new compounds and materials with reversible light‐induced change in properties have been synthesized and used in manifold applications . This includes the use in optical information storage or sunglasses or the embedding of photochromic compounds in biomacromolecules . The most prominent photochromic systems are the cis / trans ‐azobenzene and the spiropyran/merocyanine systems (Scheme ) .…”

Section: Introductionmentioning

confidence: 99%

Studies of a photochromic model system using NMR with ex‐situ and in‐situ irradiation devices

Wolff

Kind

Schenderlein

et al. 2016

Magnetic Reson in Chemistry

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The switching behavior of a photochromic model system was investigated in detail via NMR spectroscopy in order to improve understanding of the compound itself and to provide ways to obtain insights into composition trends of a photo switchable (polymeric) material containing spiropyran/merocyanine units. In addition to the classical irradiation performed outside the magnet (ex-situ), a device for irradiation inside the NMR spectrometer (in-situ) was tested. Both setups are introduced, their advantages and disadvantages as well as their limits are described and the setup for future investigations of photochromic materials is suggested. The influence of different sample concentrations, irradiation procedures, and light intensities on the model system was examined as well as the dependence on solvent, temperature, and irradiation wavelengths. Using the recently published LED illumination device, it was even possible to record two-dimensional spectra on this model system with rather short half-life (7 min in DMSO). This way (13) C chemical shifts of the merocyanine form were obtained, which were unknown before. Copyright © 2016 John Wiley & Sons, Ltd.

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“…In a recent publication by the Meyer-Almes group (Figure 9.6), they described how they modified several alkylmaleimides of varying chain length with an azobenzene system, and then covalently attached the resulting photochromic assembly to a predetermined site on a mutant histone deacetylase-like aminohydrolase (HDAH) [52,53]. The mutant variant of HDAH (M30S) contains a maleimide-reactive cysteine along the edge of an outward facing solvent loop, adjacent to the active site of the enzyme.…”

Section: Site-selective Introduction Of Photochromic Species -Single mentioning

confidence: 99%

“…(a) Azobenzene-modified maleimide of varying alkyl chain linkage length[52]. (b) Histone deacetylase-like aminohydrolase (HDAH) enzyme, active site, and external loop of enzyme mutation site.…”

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confidence: 99%