Recommendations for performing measurements of apparent equilibrium constants of enzyme-catalyzed reactions and for reporting the results of these measurements

• Robert N. Goldberg,
• Robert T. Giessmann,
• Peter J. Halling,
• Carsten Kettner and
• Hans V. Westerhoff

Beilstein J. Org. Chem. 2023, 19, 303–316, doi:10.3762/bjoc.19.26

• constants and certain enzyme kinetics parameters via the Haldane relationships. These relationships are discussed in references [10][36] and, in fact, values of K′ have been obtained for a fair number of enzyme-catalyzed reactions by measuring rates of reaction and obtaining the enzyme kinetic parameters

Kinetics of enzyme-catalysed desymmetrisation of prochiral substrates: product enantiomeric excess is not always constant

• Peter J. Halling

Beilstein J. Org. Chem. 2021, 17, 873–884, doi:10.3762/bjoc.17.73

• the ultimate equilibrium value of 0, although the timescale for this depends on details of the enzyme kinetics. To understand the range of possible behaviour, progress curves for the conversion and the ee were calculated for a wide variety of possible enzyme kinetic parameters. The calculation used

• more informative to consider the behaviour as a function of groups that each combine several elementary rate constants, as normal in enzyme kinetics. Firstly, there are constraints that mean the enzyme cannot vary all these rate constants independently. A Haldane relationship makes a combination of

Acyl-group specificity of AHL synthases involved in quorum-sensing in Roseobacter group bacteria

• Lisa Ziesche,
• Jan Rinkel,
• Jeroen S. Dickschat and
• Stefan Schulz

Beilstein J. Org. Chem. 2018, 14, 1309–1316, doi:10.3762/bjoc.14.112

• different enzyme kinetics for the PCE substrates. In contrast, in the single-substrate incubation experiments (Table 3) an excess of SAM was used, and this may have led to the formation even of products that are disfavored in the competition experiments. Conclusion The results showed that the enzymes

Synthesis and enzymatic ketonization of the 5-(halo)-2-hydroxymuconates and 5-(halo)-2-hydroxy-2,4-pentadienoates

• Tyler M. M. Stack,
• William H. Johnson Jr. and
• Christian P. Whitman

Beilstein J. Org. Chem. 2017, 13, 1022–1031, doi:10.3762/bjoc.13.101

• . The implications of these findings are discussed. The availability of these compounds will facilitate future studies of the haloaromatic catabolic pathways. Keywords: dienol; enzyme kinetics; fluoride; halogen; Introduction Aromatic hydrocarbons and their halogenated derivatives are well known

Organic chemistry meets polymers, nanoscience, therapeutics and diagnostics

• Vincent M. Rotello

Beilstein J. Org. Chem. 2016, 12, 1638–1646, doi:10.3762/bjoc.12.161

• complex behaves differently than either of the two components. A prime example of this synergy is when we showed that nanoparticle–enzyme complexes showed altered substrate selectivity [51], with the particle dictating the enzyme kinetics by acting as a "filter" for substrate and product [47]. Another

Azobenzene-based inhibitors of human carbonic anhydrase II

• Leander Simon Runtsch,
• David Michael Barber,
• Peter Mayer,
• Michael Groll,
• Dirk Trauner and
• Johannes Broichhagen

Beilstein J. Org. Chem. 2015, 11, 1129–1135, doi:10.3762/bjoc.11.127

• of the synthesized azobenzenes, we found that the electronic structure does not strongly affect inhibition. Taken together, all compounds are strong blockers of hCAII with Ki = 25–65 nM that are potentially photochromic and thus combine studies from chemical synthesis, crystallography and enzyme

• kinetics. Keywords: azobenzene chemistry; enzyme inhibitors; human carbonic anhydrase II; sulfonamide; X-ray crystallography; Introduction Carbonic anhydrase (CA) is an ubiquitously found zinc-containing metalloenzyme with many isoforms, which all catalyze the conversion of carbon dioxide and water to

3-Glucosylated 5-amino-1,2,4-oxadiazoles: synthesis and evaluation as glycogen phosphorylase inhibitors

• Marion Donnier-Maréchal,
• David Goyard,
• Vincent Folliard,
• Tibor Docsa,
• Pal Gergely,
• Jean-Pierre Praly and
• Sébastien Vidal

Beilstein J. Org. Chem. 2015, 11, 499–503, doi:10.3762/bjoc.11.56

• -1,2,4-oxadiazoles. Synthesis of 3-glucosyl-5-amino-1,2,4-oxadiazoles. Supporting Information Supporting Information File 232: Experimental details and NMR data for all new compounds as well as enzyme kinetics (IC50) measurements. Acknowledgements Financial support from CNRS, University Claude-Bernard

Enaminones in a multicomponent synthesis of 4-aryldihydropyridines for potential applications in photoinduced intramolecular electron-transfer systems

• Nouria A. Al-Awadi,
• Maher R. Ibrahim,
• Mohamed H. Elnagdi,
• Elizabeth John and
• Yehia A. Ibrahim

Beilstein J. Org. Chem. 2012, 8, 441–447, doi:10.3762/bjoc.8.50

• in the mapping of enzyme kinetics by means of the fluorescence similarity to NADH [11][12][13]. Moreover, there has been recent interest in the synthesis of dihydropyridine derivatives, due to their wide range of biological activity [14][15], by a one-pot three-component reaction with aliphatic

Hybrid biofunctional nanostructures as stimuli-responsive catalytic systems

• Gernot U. Marten,
• Thorsten Gelbrich and
• Annette M. Schmidt

Beilstein J. Org. Chem. 2010, 6, 922–931, doi:10.3762/bjoc.6.98

• of free trypsin, and redispersed in HEPES buffer. Determination of immobilized enzyme kinetics and activity: BAPNA was used as the model substrate. Four HEPES buffered BAPNA solutions with concentrations between 2.0 mM and 0.5 mM, and a 6.0 μM trypsin solution were prepared and tempered to the