Athel Cornish-Bowden

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Athel Cornish-Bowden
Athel Cornish-Bowden in 2014.jpg
Born
Athelstan John Cornish-Bowden

(1943-04-03) 3 April 1943 (age 81)
NationalityBritish, French
Education Oxford University
Known for Enzyme Kinetics, Metabolic Control Analysis
Spouse(s)Mary Ann Reynolds, María de la Luz Cárdenas Cerda
AwardsD.Sc., Oxford, 1983; corresponding member of the Academia Chilena de Ciencias
Scientific career
FieldsBiochemistry, theoretical biology
Institutions University of California, Berkeley, University of Birmingham, CNRS, Marseilles
Thesis Studies of Pepsin catalysis  (1967)
Doctoral advisor Jeremy R. Knowles
Other academic advisors Daniel E. Koshland Jr.
Signature
Signature of Athel Cornish-Bowden.jpg

Athel Cornish-Bowden (born 3 April 1943) is a British biochemist known for his numerous textbooks, particularly those on enzyme kinetics and his work on metabolic control analysis.

Contents

Education and career

Athel Cornish-Bowden worked on pepsin catalysis. [1] This began a life long pursuit of work on enzyme catalysis [2] and in later years work on the control of metabolism. [3] More recently he has also turned his attention to work related to the origin and nature of life. [4]

He obtained his D.Phil. at Oxford with Jeremy R. Knowles, [5] and carried out post-doctoral work with Daniel E. Koshland Jr. [6]

Research

Cornish-Bowden has authored over 200 peer-reviewed papers and nine textbooks [7] [8] on topics related to enzyme kinetics, mathematics and historical perspectives in science. According to Google Scholar, the textbook, Fundamentals of enzyme kinetics, [9] has been cited over 3000 times by secondary sources. [10]

Cornish-Bowden's research can be divided into three primary areas: Enzyme kinetics, metabolic control, done mainly in collaboration with Jannie Hofmeyr, and the origin of life. The following lists some of the topics and selected references to the work carried out and published by Cornish-Bowden:

Additionally, Cornish-Bowden has published a number of history of science papers commemorating the lives and achievements of historical figures in enzymology. [31] [32] [33] His current interests include the definition of life and the capacity for life to self-organize.

Major Research Contributions

Cornish-Bowden is most well known for his introduction of the direct-linear plot for estimating enzyme parameters, [34] his work on Hexokinase evolution and kinetics, [35] and his insight into the control and regulation of metabolism. [36]

Cornish-Bowden has participated on the editorial boards of various journals (the Biochemical Journal, the Journal of Theoretical Biology, FEBS Journal, BioSystems), and has been active on International Committees. He was secretary of the IUPAC-IUBMB Joint Committee on Biochemical Nomenclature [37] and in that capacity convened the committee that prepared the current IUBMB recommendations on enzyme kinetics. [38] He also contributed to recommendations on biochemical thermodynamics, [39] and to proposals for system representation of biochemical networks. [40]

Books

Fundamentals of Enzyme Kinetics

Related Research Articles

<span class="mw-page-title-main">Enzyme</span> Large biological molecule that acts as a catalyst

Enzymes are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties.

<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 a differential equation describing the reaction rate to , the concentration of the substrate A. Its formula is given by the Michaelis–Menten equation:

Robert Rosen was an American theoretical biologist and Professor of Biophysics at Dalhousie University.

<span class="mw-page-title-main">Maud Menten</span> Canadian physician and chemist (1879–1960)

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 written language of German into English.

<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.

<span class="mw-page-title-main">Henrik Kacser</span> Hungarian biochemist and geneticist

Henrik Kacser FRSE was a Austro-Hungarian-born biochemist and geneticist who worked in Britain in the 20th century. Kacser's achievements have been recognised by his election to the Royal Society of Edinburgh in 1990, by an honorary doctorate of the University of Bordeaux II in 1993.

<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.

Moiety conservation is the conservation of a subgroup in a chemical species, which is cyclically transferred from one molecule to another. In biochemistry, moiety conservation can have profound effects on the system's dynamics.

<span class="mw-page-title-main">Aldo-keto reductase family 1, member A1</span> Mammalian protein found in Homo sapiens

Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. AKR1A1 belongs to the aldo-keto reductase (AKR) superfamily. It catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols and catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Mutations in the AKR1A1 gene has been found associated with non-Hodgkin's lymphoma.

<span class="mw-page-title-main">AKR1C4</span> Protein-coding gene in the species Homo sapiens

Aldo-keto reductase family 1 member C4, also known as 3α-Hydroxysteroid dehydrogenase type 1 (3α-HSD1), is an enzyme that in humans is encoded by the AKR1C4 gene. It is known to be necessary for the synthesis of the endogenous neurosteroids allopregnanolone, tetrahydrodeoxycorticosterone, and 3α-androstanediol. It is also known to catalyze the reversible conversion of 3α-androstanediol (5α-androstane-3α,17β-diol) to dihydrotestosterone and vice versa.

Jeremy Randall Knowles was a professor of chemistry at Harvard University who served as dean of the Harvard University faculty of arts and sciences (FAS) from 1991 to 2002. He joined Harvard in 1974, received many awards for his research, and remained at Harvard until his death, leaving the faculty for a decade to serve as Dean. Knowles died on 3 April 2008 at his home.

<span class="mw-page-title-main">Chemoton</span> Abstract model for the fundamental unit of life

The term chemoton refers to an abstract model for the fundamental unit of life introduced by Hungarian theoretical biologist Tibor Gánti. Gánti conceived the basic idea in 1952 and formulated the concept in 1971 in his book The Principles of Life. He suggested that the chemoton was the original ancestor of all organisms.

<span class="mw-page-title-main">Stefan Schuster</span> German biophysicist

Stefan Schuster is a German biophysicist. He is professor for bioinformatics at the University of Jena.

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. 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.

Jan-Hendrik HofmeyrFRSSAf is one of the leaders in the field of metabolic control analysis and the quantitative analysis of metabolic regulation.

Herbert M. Sauro is a Welsh biochemist who works in the field of metabolic control analysis and systems biology.

In biochemistry, a rate-limiting step is a step that controls the rate of a series of biochemical reactions. The statement is, however, a misunderstanding of how a sequence of enzyme catalyzed reaction steps operate. Rather than a single step controlling the rate, it has been discovered that multiple steps control the rate. Moreover, each controlling step controls the rate to varying degrees.

The classic Monod–Wyman–Changeux model (MWC) for cooperativity is generally published in an irreversible form. That is, there are no product terms in the rate equation which can be problematic for those wishing to build metabolic models since there are no product inhibition terms. However, a series of publications by Popova and Sel'kov derived the MWC rate equation for the reversible, multi-substrate, multi-product reaction.

References

  1. Cornish-Bowden, AJ; Greenwell, P; Knowles, JR (June 1969). "The rate-determining step in pepsin-catalysed reactions, and evidence against an acyl-enzyme intermediate". The Biochemical Journal. 113 (2): 369–75. doi:10.1042/bj1130369. PMC   1184644 . PMID   4897200.
  2. Cornish-Bowden, A; Connolly, BA; Gregoriou, M; Holroyde, MJ; Storer, AC; Trayer, IP (December 1979). "Mammalian hexokinases: a system for the study of co-operativity in monomeric enzymes". Archivos de Biología y Medicina Experimentales. 12 (5): 581–5. PMID   552244.
  3. Hofmeyr, JH; Cornish-Bowden, A (15 August 1991). "Quantitative assessment of regulation in metabolic systems". European Journal of Biochemistry. 200 (1): 223–36. doi: 10.1111/j.1432-1033.1991.tb21071.x . PMID   1879427.
  4. Cornish-Bowden, A; Cárdenas, ML (7 December 2017). "Life before LUCA". Journal of Theoretical Biology. 434: 68–74. Bibcode:2017JThBi.434...68C. doi:10.1016/j.jtbi.2017.05.023. PMID   28536033.
  5. Cornish-Bowden, AJ; Greenwell, P; Knowles, JR (June 1969). "The rate-determining step in pepsin-catalysed reactions, and evidence against an acyl-enzyme intermediate". The Biochemical Journal. 113 (2): 369–75. doi:10.1042/bj1130369. PMC   1184644 . PMID   4897200.
  6. Cornish-Bowden, A; Koshland DE, Jr (18 August 1970). "A general method for the quantitative determination of saturation curves for multisubunit proteins". Biochemistry. 9 (17): 3325–36. doi:10.1021/bi00819a006. PMID   4330854.
  7. Silverberg, Michael (1997). "Review of Fundamentals of Enzyme Kinetics.; Analysis of Enzyme Kinetic Data". The Quarterly Review of Biology. 72 (3): 318-220. doi:10.1086/419873.
  8. Patrick, Wayne (2017). "Biochemical Evolution: The Pursuit of Perfection by Athel Cornish-Bowden". The Quarterly Review of Biology. 92 (3): 92–93. doi:10.1086/419873.
  9. Cornish-Bowden, Athel (2013). Fundamentals of Enzyme Kinetics. John Wiley & Sons.
  10. "Google Scholar".
  11. Cornish-Bowden, AJ; Knowles, JR (June 1969). "The pH-dependence of pepsin-catalysed reactions". The Biochemical Journal. 113 (2): 353–62. doi:10.1042/bj1130353. PMC   1184642 . PMID   4897198.
  12. Cornish-Bowden, AJ; Greenwell, P; Knowles, JR (June 1969). "The rate-determining step in pepsin-catalysed reactions, and evidence against an acyl-enzyme intermediate". The Biochemical Journal. 113 (2): 369–75. doi:10.1042/bj1130369. PMC   1184644 . PMID   4897200.
  13. Cornish-Bowden, A; Koshland DE, Jr (10 December 1970). "The influence of binding domains on the nature of subunit interactions in oligomeric proteins. Application to unusual kinetic and binding patterns". The Journal of Biological Chemistry. 245 (23): 6241–50. doi: 10.1016/S0021-9258(18)62600-6 . PMID   5484808.
  14. Cornish-Bowden, A; Koshland DE, Jr (18 August 1970). "A general method for the quantitative determination of saturation curves for multisubunit proteins". Biochemistry. 9 (17): 3325–36. doi:10.1021/bi00819a006. PMID   4330854.
  15. Cornish-Bowden, A; Koshland DE, Jr (25 June 1975). "Diagnostic uses of the Hill (Logit and Nernst) plots". Journal of Molecular Biology. 95 (2): 201–12. doi:10.1016/0022-2836(75)90390-3. PMID   171413.
  16. Cornish-Bowden, A (May 1975). "Letter: The physiological significance of negative co-operativity". Journal of Theoretical Biology. 51 (1): 233–5. doi:10.1016/0022-5193(75)90149-6. PMID   1142781.
  17. Coleman, KJ; Cornish-Bowden, A; Cole, JA (1 November 1978). "Purification and properties of nitrite reductase from Escherichia coli K12". The Biochemical Journal. 175 (2): 483–93. doi:10.1042/bj1750483. PMC   1186095 . PMID   217342.
  18. Jackson, RH; Cole, JA; Cornish-Bowden, A (1 May 1982). "The steady state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. The reduction of single-electron acceptors". The Biochemical Journal. 203 (2): 505–10. doi:10.1042/bj2030505. PMC   1158256 . PMID   6288003.
  19. Buc, J; Santini, CL; Blasco, F; Giordani, R; Cárdenas, ML; Chippaux, M; Cornish-Bowden, A; Giordano, G (15 December 1995). "Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants with altered beta subunits". European Journal of Biochemistry. 234 (3): 766–72. doi: 10.1111/j.1432-1033.1995.766_a.x . PMID   8575433.
  20. Cornish-Bowden, A (15 February 1976). "The effect of natural selection on enzymic catalysis". Journal of Molecular Biology. 101 (1): 1–9. doi:10.1016/0022-2836(76)90062-0. PMID   1255718.
  21. Cornish-Bowden, A (1985). "Are introns structural elements or evolutionary debris?". Nature. 313 (6002): 434–5. doi: 10.1038/313434b0 . PMID   3969152.
  22. Hofmeyr, JH; Cornish-Bowden, A (15 August 1991). "Quantitative assessment of regulation in metabolic systems". European Journal of Biochemistry. 200 (1): 223–36. doi: 10.1111/j.1432-1033.1991.tb21071.x . PMID   1879427.
  23. Cornish-Bowden, A; Hofmeyr, JH (1 March 1994). "Determination of control coefficients in intact metabolic systems". The Biochemical Journal. 298 ( Pt 2) (2): 367–75. doi:10.1042/bj2980367. PMC   1137949 . PMID   8135743.
  24. Hofmeyr, JH; Cornish-Bowden, A (7 October 1996). "Co-response analysis: a new experimental strategy for metabolic control analysis". Journal of Theoretical Biology. 182 (3): 371–80. Bibcode:1996JThBi.182..371H. doi:10.1006/jtbi.1996.0176. PMID   8944170.
  25. Hofmeyr, JS; Cornish-Bowden, A (30 June 2000). "Regulating the cellular economy of supply and demand". FEBS Letters. 476 (1–2): 47–51. doi: 10.1016/s0014-5793(00)01668-9 . PMID   10878248.
  26. Cornish-Bowden, A; Hofmeyr, JH (21 May 2002). "The role of stoichiometric analysis in studies of metabolism: an example". Journal of Theoretical Biology. 216 (2): 179–91. Bibcode:2002JThBi.216..179C. doi:10.1006/jtbi.2002.2547. PMID   12079370.
  27. Cornish-Bowden, A; Cárdenas, ML; Letelier, JC; Soto-Andrade, J; Abarzúa, FG (December 2004). "Understanding the parts in terms of the whole". Biology of the Cell. 96 (9): 713–7. doi: 10.1016/j.biolcel.2004.06.006 . PMID   15567526.
  28. Cornish-Bowden, A; Cárdenas, ML (October 2007). "Organizational invariance in (M,R)-systems". Chemistry & Biodiversity. 4 (10): 2396–406. doi:10.1002/cbdv.200790195. PMID   17955465. S2CID   6772968.
  29. Cornish-Bowden, A; Cárdenas, ML (7 June 2008). "Self-organization at the origin of life". Journal of Theoretical Biology. 252 (3): 411–8. Bibcode:2008JThBi.252..411C. doi:10.1016/j.jtbi.2007.07.035. PMID   17889904.
  30. Cárdenas, ML; Letelier, JC; Gutierrez, C; Cornish-Bowden, A; Soto-Andrade, J (7 March 2010). "Closure to efficient causation, computability and artificial life" (PDF). Journal of Theoretical Biology. 263 (1): 79–92. Bibcode:2010JThBi.263...79L. doi:10.1016/j.jtbi.2009.11.010. hdl: 10533/130547 . PMID   19962389.
  31. Cornish-Bowden, AJ; Lagnado, J (December 2013). "Maud Leonora Menten: A woman at the dawn of biochemistry". The Biochemist. 35 (6): 46–47. doi: 10.1042/BIO03506046 .
  32. Deichmann, U; Schuster, S; Mazat, J-P; Cornish-Bowden, A (January 2014). "Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives". The FEBS Journal. 81 (2): 435–463. doi: 10.1111/febs.12598 .
  33. Cornish-Bowden, AJ (March 2015). "One hundred years of Michaelis–Menten kinetics". Perspectives in Science. 4: 3–9. doi: 10.1016/j.pisc.2014.12.002 .
  34. Eisenthal, R; Cornish-Bowden, A (June 1974). "The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters". The Biochemical Journal. 139 (3): 715–20. doi:10.1042/bj1390715. PMC   1166335 . PMID   4854723.
  35. Cárdenas, ML; Cornish-Bowden, A; Ureta, T (5 March 1998). "Evolution and regulatory role of the hexokinases". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1401 (3): 242–64. doi: 10.1016/s0167-4889(97)00150-x . PMID   9540816.
  36. Hofmeyr, JS; Cornish-Bowden, A (30 June 2000). "Regulating the cellular economy of supply and demand". FEBS Letters. 476 (1–2): 47–51. doi: 10.1016/s0014-5793(00)01668-9 . PMID   10878248.
  37. Dixon, H B F; Cornish-Bowden, A (1983). "Revision of Enzyme Nomenclature — Listing Enzymes". Eur. J. Biochem. 133 (3): 479. doi:10.1111/j.1432-1033.1983.tb07489.x.
  38. Nomenclature Committee of the International Union of Biochemistry (NC-IUB) (1983). "Symbolism and terminology in enzyme kinetics: recommendations 1981". Arch. Biochem. Biophys. 224 (2): 732–740. doi:10.1016/0003-9861(83)90262-X.
  39. Alberty, R A; Cornish-Bowden, A; Goldberg, R N; Tipton, K F; Westerhoff, H V (2011). "Recommendations for terminology and databases for biochemical thermodynamics". Biophys. Chem. 155 (2–3): 89–103. doi:10.1016/j.bpc.2011.03.007. PMID   21501921.
  40. Hucka, A.; Finney, H. M.; Sauro, H.; Bolouri, J. C.; Doyle, H.; Kitano, A. P.; et al. (2003). "The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models". Bioinformatics. 19 (4): 524–531. doi:10.1093/bioinformatics/btg015. PMID   12611808.