The STRENDA Guidelines

Both the STRENDA project and the STRENDA Guidelines are registered in, a web portal that collects interrelated data standards, databases, and policies in the life, environmental and biomedical sciences.

Today more than 50 international biochemistry journals recommend their authors to consult the STRENDA Guidelines when publishing enzyme kinetics data.

The STRENDA Guidelines aim to support authors to comprehensively report kinetic and equilibrium data from their investigations of enzymeactivities. However, STRENDA aims neither to dictate or limit the experimental techniques used in enzymology experiments nor to establish a metric for judging the quality of experimental data. The emphasis is on providing useful and reliable information.

The full Guidelines are accessible here:

Overview. The following parameters need to be provided in scientific publications: All reports of kinetic and binding data must include a description of the identity of the catalytic or binding entity (enzyme, protein, nucleic acid or other molecule). This information should include the origin or source of the molecule, its purity, composition, and other characteristics such as post-translational modifications, mutations, and any modifications made to facilitate expression or purification. The assay methods and exact experimental conditions of the assay must be fully described if it is a new assay or provided as a reference to previously published work, with or without modifications.

The temperature, pH and pressure (if other than atmospheric) of the assay must always be included, even if previously published. In instances where catalytic activity or binding cannot be detected, an estimate of the limit of detection based on the sensitivity and error analysis of the assay should be provided. Ambiguous terms such as "not detectable" should be avoided. A description of the software used for data analysis should be included along with calculated errors for all parameters.

First-order and second-order rate constants should be reported in units of s-1 and M-1•s-1, respectively. Equilibrium binding constants should normally bereported as dissociation constants with units of concentration (M, mM, µM, nM). The values kcat, kcat/Km and Km from steady-state enzyme kinetics should be reported in units of s-1, M-1•s-1 and concentration (mM, µM, nM), respectively. The steady-state specific activity of an enzyme should normally be reported as a kcat. If there is considerable uncertainty in the molar concentration of the catalyst, the specific activity should be reported as a Vmax (nmol, µmol) of product formed per amount of protein per unit time (e.g. µmol•mg-1•s-1).