Standards for Reporting Enzymology Data

Last updated

Standards for Reporting Enzymology Data (STRENDA) is an initiative as part of the Minimum Information Standards which specifically focuses on the development of guidelines for reporting (describing metadata) enzymology experiments. The initiative is supported by the Beilstein Institute for the Advancement of Chemical Sciences. [1] STRENDA establishes both publication standards for enzyme activity data and STRENDA DB, an electronic validation and storage system for enzyme activity data. Launched in 2004, the foundation of STRENDA is the result of a detailed analysis of the quality of enzymology data in written and electronic publications. [2] [3]

Contents

Organization

The STRENDA project is driven by 15 scientists from all over the world forming the STRENDA Commission [4] and supporting the work with expertises in biochemistry, enzyme nomenclature, bioinformatics, systems biology, modelling, mechanistic enzymology and theoretical biology.

Reporting guidelines

The STRENDA Guidelines [5] propose those minimum information that is needed to comprehensively report kinetic and equilibrium data from investigations of enzyme activities including corresponding experimental conditions. This minimum information is suggested to be addressed in a scientific publication when enzymology research data is reported to ensure that data sets are comprehensively described. This allows scientists not only to review, interpret and corroborate the data but also to reuse the data for modelling and simulation of biocatalytic pathways. In addition, the guidelines support researchers making their experimental data reproducible and transparent. [6] [7] [8] [9]

As of March 2020, more than 55 international biochemistry journal included the STRENDA Guidelines in their authors' instructions as recommendations when reporting enzymology data. [10] The STRENDA project is registered with FAIRsharing.org [11] and the Guidelines are part of the FAIRDOM Community standards for Systems Biology. [12]

Applications

STRENDA DB

STRENDA DB [13] is a web-based storage and search platform that has incorporated the Guidelines and automatically checks the submitted data on compliance with the STRENDA Guidelines thus ensuring that the manuscript data sets are complete and valid. A valid data set is awarded a STRENDA Registry Number (SRN) and a fact sheet (PDF) is created containing all submitted data. Each dataset is registered at Datacite and assigned a DOI to refer and track the data. After the publication of the manuscript in a peer-reviewed journal the data in STRENDA DB are made open accessible. [14] [15] STRENDA DB is a repository recommended by re3data and OpenDOAR. It is harvested by OpenAIRE. The database service is recommended in the authors' instructions of more than 10 biochemistry journals, including Nature, The Journal of Biological Chemistry, eLife, and PLoS. It has been referred as a standard tool for the validation and storage of enzyme kinetics data in multifold publications [16] [17] [18] [19] [20] [21] A recent study examining eleven publications, including Supporting Information, from two leading journals revealed that at least one omission was found in every one of these papers. The authors concluded that using STRENDA DB in the current version would ensure that about 80% auf the relevant information would be made available. [22]

Data Management

STRENDA DB is considered a tool for research data management by the research community (e.g. EU project CARBAFIN [23] ).

Related Research Articles

The katal is the unit of catalytic activity in the International System of Units (SI) used for quantifying the catalytic activity of enzymes and other catalysts.

<span class="mw-page-title-main">Hexokinase</span> Class of enzymes

A hexokinase is an enzyme that phosphorylates hexoses, forming hexose phosphate. In most organisms, glucose is the most important substrate for hexokinases, and glucose-6-phosphate is the most important product. Hexokinase possesses the ability to transfer an inorganic phosphate group from ATP to a substrate.

<span class="mw-page-title-main">Michaelis–Menten kinetics</span> Model of enzyme kinetics

In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product. It takes the form of an equation describing the rate reaction rate to , the concentration of the substrate A. Its formula is given by the Michaelis–Menten equation:

<span class="mw-page-title-main">Eduard Buchner</span> German chemist (1860–1917)

Eduard Buchner was a German chemist and zymologist, awarded the 1907 Nobel Prize in Chemistry for his work on fermentation.

<span class="mw-page-title-main">Maud Menten</span> Canadian physician and chemist

Maud Leonora Menten was a Canadian physician and chemist. As a bio-medical and medical researcher, she made significant contributions to enzyme kinetics and histochemistry and invented a procedure that remains in use. She is primarily known for her work with Leonor Michaelis on enzyme kinetics in 1913. The paper has been translated from its original German into English.

Products are the species formed from chemical reactions. During a chemical reaction, reactants are transformed into products after passing through a high energy transition state. This process results in the consumption of the reactants. It can be a spontaneous reaction or mediated by catalysts which lower the energy of the transition state, and by solvents which provide the chemical environment necessary for the reaction to take place. When represented in chemical equations, products are by convention drawn on the right-hand side, even in the case of reversible reactions. The properties of products such as their energies help determine several characteristics of a chemical reaction, such as whether the reaction is exergonic or endergonic. Additionally, the properties of a product can make it easier to extract and purify following a chemical reaction, especially if the product has a different state of matter than the reactants.

<span class="mw-page-title-main">Eadie–Hofstee diagram</span> Graph of enzyme kinetics

In biochemistry, an Eadie–Hofstee plot is a graphical representation of the Michaelis–Menten equation in enzyme kinetics. It has been known by various different names, including Eadie plot, Hofstee plot and Augustinsson plot. Attribution to Woolf is often omitted, because although Haldane and Stern credited Woolf with the underlying equation, it was just one of the three linear transformations of the Michaelis–Menten equation that they initially introduced. However, Haldane indicated latter that Woolf had indeed found the three linear forms: "In 1932, Dr. Kurt Stern published a German translation of my book "Enzymes", with numerous additions to the English text. On pp. 119-120, I described some graphical methods, stating that they were due to my friend Dr. Barnett Woolf. [...] Woolf pointed out that linear graphs are obtained when is plotted against , against , or against , the first plot being most convenient unless inhibition is being studied."

Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate. This is unlike allosteric inhibition, where binding affinity for the substrate in the enzyme is decreased in the presence of an inhibitor.

Turnover number has two different meanings:

<span class="mw-page-title-main">Enzyme kinetics</span> Study of biochemical reaction rates catalysed by an enzyme

Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier might affect the rate.

<span class="mw-page-title-main">Robert A. Alberty</span> American chemist (1921–2014)

Robert Arnold Alberty (1921-2014) was an American biophysical chemist, Professor Emeritus at the Massachusetts Institute of Technology, and a member of the National Academy of Sciences.

Uncompetitive inhibition is a type of inhibition in which the apparent values of the Michaelis–Menten parameters and are decreased in the same proportion.

<span class="mw-page-title-main">Adrian John Brown</span>

Adrian John Brown, FRS was a British Professor of Malting and Brewing at the University of Birmingham and a pioneer in the study of enzyme kinetics.

Hans Lineweaver was an American physical chemist, who is credited with introducing the double-reciprocal plot or Lineweaver–Burk plot. The paper containing the equation was co-authored by Dean Burk, and was entitled "The Determination of Enzyme Dissociation Constants (1934)". It remains the most frequently cited paper to appear in the Journal of the American Chemical Society. Lineweaver and Burk collaborated with the eminent statistician W. Edwards Deming on the statistical analysis of their data: they used the plot for illustrating the results, not for the analysis itself.

Santiago Schnell FRSC is a Venezuelan theoretical and mathematical biologist. He is the William K. Warren Foundation Dean of the College of Science at the University of Notre Dame, as well as a professor in the Department of Biological Sciences, and Department of Applied and Computational Mathematics and Statistics. Before this, he was the Chair of the Department of Molecular & Integrative Physiology and the John A. Jacquez Collegiate Professor of Physiology at the University of Michigan. He was also Professor of Computational Medicine & Bioinformatics at the same institution.

<span class="mw-page-title-main">Enzyme Function Initiative</span> Collaborative project to determine enzyme function

The Enzyme Function Initiative (EFI) is a large-scale collaborative project aiming to develop and disseminate a robust strategy to determine enzyme function through an integrated sequence–structure-based approach. The project was funded in May 2010 by the National Institute of General Medical Sciences as a Glue Grant which supports the research of complex biological problems that cannot be solved by a single research group. The EFI was largely spurred by the need to develop methods to identify the functions of the enormous number proteins discovered through genomic sequencing projects.

<span class="mw-page-title-main">SABIO-Reaction Kinetics Database</span>

SABIO-RK is a web-accessible database storing information about biochemical reactions and their kinetic properties.

<span class="mw-page-title-main">Asparagine synthase (glutamine-hydrolysing)</span>

Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent asparagine synthetase, asparagine synthetase B, AS, AS-B) is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming). This enzyme catalyses the following chemical reaction

The Minimum Information Required About a Glycomics Experiment (MIRAGE) initiative is part of the Minimum Information Standards and specifically applies to guidelines for reporting on a glycomics experiment. The initiative is supported by the Beilstein Institute for the Advancement of Chemical Sciences. The MIRAGE project focuses on the development of publication guidelines for interaction and structural glycomics data as well as the development of data exchange formats. The project was launched in 2011 in Seattle and set off with the description of the aims of the MIRAGE project.

<span class="mw-page-title-main">Athel Cornish-Bowden</span> British biochemist

Athel Cornish-Bowden is a British biochemist known for his numerous textbooks, particularly those on enzyme kinetics and his work on metabolic control analysis.

References

  1. "Strenda - Projects - Beilstein-Institut zur Förderung der Chemischen Wissenschaften". www.beilstein-institut.de.
  2. Kettner, Carsten; Hicks, Martin (1 June 2005). "The Dilemma of Modern Functional Enzymology". Current Enzyme Inhibition. 1 (2): 171–181. doi:10.2174/1573408054022234.
  3. Apweiler, R; Cornish-Bowden, A; Hofmeyr, JH; Kettner, C; Leyh, TS; Schomburg, D; Tipton, K (January 2005). "The importance of uniformity in reporting protein-function data". Trends in Biochemical Sciences. 30 (1): 11–2. doi:10.1016/j.tibs.2004.11.002. PMID   15653320.
  4. "Commission - Strenda - Projects - Beilstein-Institut zur Förderung der Chemischen Wissenschaften". www.beilstein-institut.de.
  5. "Guidelines - Strenda - Projects - Beilstein-Institut zur Förderung der Chemischen Wissenschaften". www.beilstein-institut.de.
  6. Tipton, Keith F.; Armstrong, Richard N.; Bakker, Barbara M.; Bairoch, Amos; Cornish-Bowden, Athel; Halling, Peter J.; Hofmeyr, Jan-Hendrik; Leyh, Thomas S.; Kettner, Carsten; Raushel, Frank M.; Rohwer, Johann; Schomburg, Dietmar; Steinbeck, Christoph (May 2014). "Standards for Reporting Enzyme Data: The STRENDA Consortium: What it aims to do and why it should be helpful". Perspectives in Science. 1 (1–6): 131–137. doi: 10.1016/j.pisc.2014.02.012 .
  7. Gardossi, Lucia; Poulsen, Pout B.; Ballesteros, Antonio; Hult, Karl; Svedas, Vytas K.; Vasic-Racki, Durda; Carrea, Giacomo; Magnusson, Anders; Schmid, Andreas; Wohlgemuth, Roland; Halling, Peter J. (April 2010). "Guidelines for reporting of biocatalytic reactions". Trends in Biotechnology. 28 (4): 171–180. doi:10.1016/j.tibtech.2010.01.001. PMID   20149467.
  8. Erb, Tobias J. (February 2019). "Back to the future: Why we need enzymology to build a synthetic metabolism for the future". Beilstein Journal of Organic Chemistry. 15: 551–557. doi: 10.3762/bjoc.15.49 . PMC   6404388 . PMID   30873239. S2CID   76665217.
  9. Gygli, Gudrun; Pleiss, Juergen (April 2020). "Simulation Foundry: Automated and FAIR molecular modeling". Journal of Chemical Information and Modeling. 60 (4): 1922–1927. doi:10.1021/acs.jcim.0c00018. PMID   32240586. S2CID   214772277.
  10. "Journals - Strenda - Projects - Beilstein-Institut zur Förderung der Chemischen Wissenschaften". www.beilstein-institut.de.
  11. FAIRsharing Team (2015). "STRENDA at FAIRsharing.org". FAIRsharing. doi:10.25504/FAIRsharing.8ntfwm.{{cite journal}}: Cite journal requires |journal= (help)
  12. "FAIRDOM Community Standards for Systems Biology".
  13. "STRENDA DB Home". www.beilstein-strenda-db.org.
  14. Apweiler, Rolf; Armstrong, Richard; Bairoch, Amos; Cornish-Bowden, Athel; Halling, Peter J; Hofmeyr, Jan-Hendrik S; Kettner, Carsten; Leyh, Thomas S; Rohwer, Johann; Schomburg, Dietmar; Steinbeck, Christoph; Tipton, Keith (18 October 2010). "A large-scale protein-function database". Nature Chemical Biology. 6 (11): 785. doi: 10.1038/nchembio.460 . PMC   3245624 . PMID   20956966.
  15. Swainston, Neil; Baici, Antonio; Bakker, Barbara M.; Cornish‐Bowden, Athel; Fitzpatrick, Paul F.; Halling, Peter; Leyh, Thomas S.; O'Donovan, Claire; Raushel, Frank M.; Reschel, Udo; Rohwer, Johann M.; Schnell, Santiago; Schomburg, Dietmar; Tipton, Keith F.; Tsai, Ming‐Daw; Westerhoff, Hans V.; Wittig, Ulrike; Wohlgemuth, Roland; Kettner, Carsten (23 March 2018). "STRENDA DB: enabling the validation and sharing of enzyme kinetics data". The FEBS Journal. 285 (12): 2193–2204. doi: 10.1111/febs.14427 . PMC   6005732 . PMID   29498804.
  16. Fademrecht, Silvia; Pleiss, Jürgen (2018). "Enzymmodellierung: von der Sequenz zum Substratkomplex". Einführung in die Enzymtechnologie (in German). Springer. pp. 35–51. doi:10.1007/978-3-662-57619-9_3. ISBN   978-3-662-57619-9.
  17. Cornish-Bowden, Athel (2012). Fundamentals of enzyme kinetics (4th., rev. and enlarged ed.). Wiley-VCH. pp. 413–450. ISBN   978-3-527-33074-4.
  18. Emmerich, Christoph H.; Harris, Christopher M. (2020). "Minimum Information and Quality Standards for Conducting, Reporting, and Organizing In Vitro Research". Good Research Practice in Non-Clinical Pharmacology and Biomedicine. Handbook of Experimental Pharmacology. Vol. 257. Springer International Publishing. pp. 177–196. doi: 10.1007/164_2019_284 . ISBN   978-3-030-33656-1. PMID   31628600.
  19. Punekar, N. S. (2018). "Good Kinetic Practices". ENZYMES: Catalysis, Kinetics and Mechanisms. Springer. pp. 131–142. doi:10.1007/978-981-13-0785-0_13. ISBN   978-981-13-0785-0.
  20. National Academies of Sciences, Engineering (2018). Open Science by Design: Realizing a Vision for 21st Century Research. ISBN   978-0-309-47624-9.
  21. Harmer, Nicholas J.; Vega, Mirella Vivoli (2019). "Reaction Chemical Kinetics in Biology". Biomolecular and Bioanalytical Techniques. John Wiley & Sons, Ltd. pp. 179–217. doi:10.1002/9781119483977.ch9. ISBN   978-1-119-48397-7. S2CID   133422670.
  22. Halling, Peter; Fitzpatrick, Paul F.; Raushel, Frank M.; Rohwer, Johann; Schnell, Santiago; Wittig, Ulrike; Wohlgemuth, Roland; Kettner, Carsten (November 2018). "An empirical analysis of enzyme function reporting for experimental reproducibility: Missing/incomplete information in published papers". Biophysical Chemistry. 242: 22–27. doi:10.1016/j.bpc.2018.08.004. PMC   6258184 . PMID   30195215.
  23. "Documents download module". ec.europa.eu.

External References