Bengt Mannervik

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Bengt Mannervik
Born
Bengt Eriksson

(1943-08-19) 19 August 1943 (age 81)
Stockholm, Sweden
Education Norra Real, Stockholm, Stockholm University (Ph.D. 1969)
Known forStudies of enzymes involved in glutathione metabolism
Awards Björkén Prize (Uppsala University)
Scientific career
Fields Biochemistry
InstitutionsStockholm University, Uppsala University, Scripps Research Institute, La Jolla, California, and many visiting appointments

Bengt Mannervik (born 19 August 1943 in Stockholm), [1] is a Swedish biochemist known especially for work on enzymes related to glutathione metabolism.

Contents

Education

After secondary education under his birth name, Bengt Eriksson, at Norra Real in Stockholm, Bengt Mannervik studied at Stockholm University [1] where he obtained his Licenciate of Philosophy in chemistry with a thesis on biochemistry in 1967. He obtained a Ph.D. there in 1969, and became a Docent (associate professor) at Stockholm University in 1970.

Career

Bengt Mannervik was Senior Lecturer in the Department of Biochemistry at Stockholm University from 1970 to 1987, and was Acting Chairman for numerous periods between 1971 and 1988. [2] In 1988 he moved to Uppsala University as holder of the Karin and Herbert Jacobsson endowed chair in biochemistry. [1] He was Chairman of the Biochemistry Department from 1998 to 2010. From 2010 to 2012 he was a Senior Professor at Uppsala University, and was a member of the university senate from 2005 to 2008. [2]

In 2010 he became Professor at Stockholm University. [3] In addition he was an adjunct professor at the Scripps Research Institute in La Jolla, California, between 2013 and 2019.

Visiting professorships

He has had visiting professorships at UC Berkeley; University of Chieti, Italy; University of Perugia, Italy; the Scripps Research Institute, La Jolla, California; and the Collège de France, Paris [2]

Professional services

He has fulfilled roles in numerous professional organizations, including the Swedish Biochemical Society (secretary 1976–1982); Chairman of the Swedish National Committee on Biochemistry, Royal Swedish Academy of Sciences, 1988–1990; Chairman Scientific Program Committee for the 22nd Meeting of the Federation of European Biochemical Societies, FEBS 1993; editorial boards of the Biochemical Journal, ChemBioChem, Biochimica et Biophysica Acta, Protein Engineering Design and Selection, the Journal of Biological Chemistry.

In addition, he has had advisory roles at various companies: Telik Inc.; PanVera Corporation, Pharmacia Biotech; Uniroyal Chemical Company; Biovitrum AB; Maxygen; Vividion; Oxford Biomedical Research, Rochester Hills, Michigan.

Research

From the beginning of his career [4] Bengt Mannervik studied enzymes of glutathione metabolism, including studies of levels in different tissues, [5] structure and catalytic activity of glutathione transferase, [6] a purification method, [7] a detailed review on the isoenzymes of glutathione transferase, [8] and many others. These publications have had a major influence on the field of glutathione biochemistry. Each of those mentioned above, together with three others, had been cited more than 1000 times by the end of 2024, the first [5] more than 5000 times, leading to an h index of 89, as calculated by Google Scholar. [9] In all he has had nearly 600 publications, with a combined total of more than 47000 citations.

His interest in glutathione transferases continued until the last years of his research, for example studies of their role as efficient ketosteroid isomerases [10] and as enzymes involved in the biosynthesis of moulting hormones in mosquitoes transmitting malaria and yellow fever. [11]

In addition to the work directed specifically at enzymes involved in glutathione metabolism and detoxication, [12] Mannervik coauthored texts on molecular toxicology. [13] [14]

He also studied various more general aspects of enzymology, including graphical analysis, [15] error structure of kinetic experiments, [16] weighting of observations, [17] [18] regression methods, [19] directed enzyme evolution, [20] and discrimination between models. [21]

Major contributions were more recently directed to the evolution of novel functions by in vitro protein evolution. [22] [23] [24]

Honours

Bengt Mannervik (born Eriksson) studied at the prestigious high school Norra Real in Stockholm and was given the prize for the best graduate in 1962. In 1988 he won the competition among 20 applicants for the internationally advertised Karin and Herbert Jacobsson Professorship of Biochemistry at Uppsala University, originally held by Nobel Prize Laureate Arne Tiselius. [1] In 2013 he was awarded the Björkén Prize of Uppsala University. [25] He was elected to the Academia Europaea in 2023. [2] He was elected to the American Association for Cancer Research, and the Royal Society of Sciences at Uppsala. He is an Honorary Member of the American Society of Biochemistry and Molecular Biology

Related Research Articles

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

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<span class="mw-page-title-main">Cofactor (biochemistry)</span> Non-protein chemical compound or metallic ion

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.

<span class="mw-page-title-main">Transferase</span> Class of enzymes which transfer functional groups between molecules

In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.

Glutathione <i>S</i>-transferase Family of enzymes

Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.

<span class="mw-page-title-main">Glutathione reductase</span> Enzyme

Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar equivalents of GSH:

<span class="mw-page-title-main">Glutathione S-transferase A1</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.

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<span class="mw-page-title-main">Steroid Delta-isomerase</span>

In enzymology, a steroid Δ5-isomerase is an enzyme that catalyzes the chemical reaction

In enzymology, a thiosulfate-thiol sulfurtransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Xenobiotic metabolism</span>

Xenobiotic metabolism is the set of metabolic pathways that modify the chemical structure of xenobiotics, which are compounds foreign to an organism's normal biochemistry, such as drugs and poisons. These pathways are a form of biotransformation present in all major groups of organisms, and are considered to be of ancient origin. These reactions often act to detoxify poisonous compounds; however, in cases such as in the metabolism of alcohol, the intermediates in xenobiotic metabolism can themselves be the cause of toxic effects.

<span class="mw-page-title-main">GSTA2</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.

<span class="mw-page-title-main">GSTM2</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene.

<span class="mw-page-title-main">GSTM3</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase M3 (brain), also known as GSTM2, is an enzyme which in humans is encoded by the GSTM99 gene.

<span class="mw-page-title-main">GSTA4</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.

<span class="mw-page-title-main">GSTZ1</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase Zeta 1 is an enzyme that in humans is encoded by the GSTZ1 gene on chromosome 14.

<span class="mw-page-title-main">GSTM4</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene.

<span class="mw-page-title-main">Microsomal glutathione S-transferase 1</span> Protein-coding gene in the species Homo sapiens

Microsomal glutathione S-transferase 1 is an enzyme that in humans is encoded by the MGST1 gene.

<span class="mw-page-title-main">GSTA3</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene.

<span class="mw-page-title-main">MGST2</span> Protein-coding gene in the species Homo sapiens

Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene.

Brian Selby Hartley FRS was a British biochemist. He was Professor of Biochemistry at Imperial College London from 1974 to 1991.

References

  1. 1 2 3 4 "Curriculum vitae" (PDF). Stockholm University. Retrieved 24 December 2024.
  2. 1 2 3 4 "Bengt Mannervik". Academia Europaea. Retrieved 27 December 2024.
  3. ↑ Stockholm University, https://www.su.se/english/profiles/bmann-1.188234
  4. ↑ Eriksson, Bengt (1966). "On the synthesis and enzymatic reduction of the coenzyme A- glutathione mixed disulfide". Acta Chem. Scand. 20 (4): 1178–1179. doi:10.3891/acta.chem.scand.20-1178. PMID   5965128.
  5. 1 2 Moron, Maria S.; Depierre, Joseph W.; Mannervik, Bengt (1979). "Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver". Biochim. Biophys. Acta. 582 (1): 67–78. doi:10.1016/0304-4165(79)90289-7. PMID   760819.
  6. ↑ Mannervik, Bengt; Danielson, U. Helena; Ketterer, Brian (1988). "Glutathione Transferases—Structure and Catalytic Activity". Crit. Rev. Biochem. 23 (3): 283–337. doi:10.3109/10409238809088226. PMID   3069329.
  7. ↑ Carlberg, Inger; Mannervik, Bengt (1985). "Glutathione reductase". Glutamate, Glutamine, Glutathione, and Related Compounds. Methods Enzymol. Vol. 113. pp. 484–490. doi:10.1016/S0076-6879(85)13062-4. ISBN   978-0-12-182013-8. PMID   3003504.
  8. ↑ Mannervik, Bengt (1985). "The isoenzymes of glutathione transferase". Advances in Enzymology and Related Areas of Molecular Biology. Vol. 57. pp. 357–417. doi:10.1002/9780470123034.ch5. ISBN   978-0-471-89011-9. PMID   3898742.{{cite book}}: |journal= ignored (help)
  9. ↑ Google Scholar: accessed 25 December 2024: https://scholar.google.com/citations?user=RymaWmIAAAAJ&hl=en&oi=ao
  10. ↑ Mannervik, Bengt; Ismail, Aram; Lindstrom, Helena; Sjödin, Birgitta; Ing, Nancy H. (2021). "Glutathione transferases as efficient ketosteroid isomerases". Front. Mol. Biosci. 8: 765970. doi: 10.3389/fmolb.2021.765970 . PMC   8645602 . PMID   34881290.
  11. ↑ Šťastná, Katarína; Musdal, Yaman; Ismail, Aram; Ebihara, Kana; Niwa, Ryusuke; Mannervik, Bengt (2024). "Supreme glutathione-dependent ketosteroid isomerase in the yellow-fever transmitting mosquito Aedes aegypti". Biochem. Biophys. Res. Comm. 711: 149914. doi: 10.1016/j.bbrc.2024.149914 . PMID   38608434.
  12. ↑ Mannervik, B., ed. (2024). Versatility of Glutathione Transferase Proteins. Basel: MDPI. ISBN   978-3-7258-0454-2.
  13. ↑ Josephy, P. D.; Mannervik, B. (2006). Molecular Toxicology. Oxford University Press.
  14. ↑ Mannervik, B.; Morgenstern, R. (2024). Glutathione transferases. Comprehensive Toxicology (4th ed.).
  15. ↑ Mannervik, Bengt (1975). "Graphical analysis of steady-state kinetic data of multireactant enzymes". Anal. Biochem. 63 (1): 12–16. doi:10.1016/0003-2697(75)90184-0. PMID   1167422.
  16. ↑ Mannervik, B.; Jakobson, I.; Warholm, M. (1986). "Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments". Biochem. J. 235 (3): 797–804. doi:10.1042/bj2350797. PMC   1146758 . PMID   3753447.
  17. ↑ Mannervik, B.; Jakobson, I.; Warholm, M. (1979). "A new procedure to derive weighting factors for nonlinear regression analysis applied to enzyme kinetic data". Biochim. Biophys. Acta. 567 (1): 43–48. doi:10.1016/0005-2744(79)90170-0. PMID   454628.
  18. ↑ Mannervik, B. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models. Contemporary Enzyme Kinetics and Mechanism (ed. D. Purich). pp. 73–94.
  19. ↑ Mannervik, B. (1975). "Nonlinear regression methods in design of experiments and mathematical modelling. Applications to the analysis of the steady-state kinetics of glutathione reductase". BioSystems. 7 (1): 101–119. Bibcode:1975BiSys...7..101M. doi:10.1016/0303-2647(75)90048-9. PMID   239774.
  20. ↑ Larsson, Anna-Karin; Emrén, Lars O.; Bardsley, William G.; Mannervik, Bengt (2004). "Directed enzyme evolution guided by multidimensional analysis of substrate-activity space". Protein Eng. Des. Sel. l17 (1): 49–55. doi:10.1093/protein/gzh005. PMID   14985537.
  21. ↑ Mannervik, Bengt; Bártfai, T. (1973). "Discrimination between mathematical models of biological systems exemplified by enzyme steady state kinetics". Acta Biol. Med. Germanica. 31 (2): 203–221. PMID   4149362.
  22. ↑ Norrgård, M. A.; Ivarsson, Y.; Tars, K.; Mannervik, B. (2006). "Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution". Proc. Natl. Acad. Sci. USA. 103 (13): 4876–4881. Bibcode:2006PNAS..103.4876N. doi: 10.1073/pnas.0600849103 . PMC   1458763 . PMID   16549767.
  23. ↑ Kurtovic, S.; Mannervik, B. (2009). "Identification of emerging quasi-species in directed enzyme evolution". Biochemistry. 48 (40): 9330–9339. doi:10.1021/bi901168q. PMID   19746988.
  24. ↑ Ismail, A.; Govindarajan, S.; Mannervik, B. (2024). "Human GST P1-1 redesigned for enhanced catalytic activity with the anticancer prodrug Telcyta and improved thermostability". Cancers. 16 (4): 762. doi: 10.3390/cancers16040762 . PMC   10887215 . PMID   38398153.
  25. ↑ "The Björkén Prize". 6 September 2024.
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