Institut de Chimie Moléculaire et des Matériaux d'Orsay

Laboratoire de Chimie Bioorganique et Bioinorganique - LCBB

 

Laurent Salmon

Laurent Salmon


Professor
Team Director

UMR 8182, ICMMO
Institut de Chimie Moléculaire et des Matériaux d’Orsay
Université Paris-Sud, Bât 420
91405 Orsay Cedex

Tel: +33 1 69 15 63 11
Fax: +33 1 69 15 72 81

send an email

Supervisor of Master M2 "Pollutions Chimiques et Gestion Environnementale" (PCGE)

Research interests: Subject 1

Aldonohydroxamic acids
and other monosaccharidic analogues: synthesis, enzymatic evaluation and structural and physico-chemical studies. Enzymes of the sugars metabolism (phosphoglucose isomerases and other aldose-ketose isomerases) : inhibition, structural and mechanistic studies.


Teaching:

Licence de biologie L3
-Chemical modifications of proteins.
Master de chimie M1
-Kinetic and mechanisms of enzymatic reactions.
Master Pro M2 Pollutions Chimiques et Gestion Environnementale (PCGE)
-Biogeochemistry and chemistry of pollutants
Master recherche M2 de Chimie Organique
Master recherche M2 Ingeniérie et Chimie des Biomolécules (ICBM)
-Kinetic, mechanisms and inhibition of enzymatic reactions.

Publications (2001-2016):

Complexes of a Zn-metalloenzyme binding site with hydroxamate-containing ligands. A case for detailed benchmarkings of polarizable molecular mechanics/dynamics potentials when the experimental binding structure is unknown.
Nohad GRESH, David PERAHIA, Benoit DE COURCY, Johanna FORET, Céline ROUX, Lea EL-KHOURY, Jean-Philip PIQUEMAL, Laurent SALMON
J. Comput. Chem. 2016, 37, 2770-2782.


Structural Basis for Competitive Inhibition of 3,4-Dihydroxy-2-Butanone-4-Phosphate Synthase from Vibrio cholerae.

Zeyaul ISLAM, Adarsh KUMAR, Suruchi SINGH, Laurent SALMON and Subramanian KARTHIKEYAN
J. Biol. Chem.
2015, 290, 11293-11308.

Exploring inhibition of Pdx1, a component of the PLP synthase complex of the human malaria parasite Plasmodium falciparum.
Shaun B. REEKSTING, Ingrid B. MULLER, Pieter B. BURGER, Emmanuel S. BURGOS, Laurent SALMON, Abraham I. LOUW, Lyn-Marie BIRKHOLTZ and Carsten WRENGER
Biochem. J. 2013, 449, 175-187.

Synthesis and evaluation of malonate-based inhibitors of phosphosugar-metabolizing enzymes : class II fructose-1,6-bis-phosphate alodolases, type I phosphomannose isomerase, and phosphoglucose isomerase.
S. DESVERGNES, S. COURTIOL-LEGOURD, R. DAHER, M. DABROWSKI, L. SALMON, M. THERISOD
Bioorg. Med. Chem. 2012, 20, 1511-1520.

Polarizable water networks in ligand-metalloprotein recognition. Impact on the relative complexation energies of Zn-dependent phosphomannose isomerase with D-mannose 6-phosphate surrogates.
N. GRESH, B. de COURCY, J.-P. PIQUEMAL, J. FORET, S. COURTIOL-LEGOURD, and L. SALMON
J. Phys. Chem. B 2011, 115, 8304-8316.

The reaction mechanism of type I phosphomannose isomerases: new information from inhibition and polarizable molecular mechanics studies.
C. ROUX, F. BHATT, J. FORET, B. de COURCY, N. GRESH, J.-P. PIQUEMAL, C. J. JEFFERY, and L. SALMON
Proteins 2011, 79, 203-220.

Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase.
M. SALIN, E. G. KAPETANIOU, M. VAISMAA, M. LAJUNEN, M. G. CASTELEIJN, P. NEUBAUER, L. SALMON, and R. K. WIERENGA
Acta Crystallogr., Sect. D: Biol. Crystallogr. 2010, 66, 934-944.

Synthesis and evaluation of non-hydrolyzable D-mannose 6-phosphate surrogates reveal 6-deoxy-6-dicarboxymethyl-D-mannose as a new strong inhibitor of phosphomannose isomerases.
J. FORET, B. de COURCY, N. GRESH, J.-P. PIQUEMAL, and L. SALMON
Bioorg. Med. Chem. 2009, 17, 7100-7107.

Competitive inhibitors of type B ribose-5-phosphate isomerases: design, synthesis and kinetic evaluation of new D-allose and D-allulose 6-phosphate derivatives.
S. MARIANO, A. K. ROOS, S. L. MOWBRAY, and L. SALMON
Carbohydr. Res. 2009, 344, 869-880.

D-Ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase while the Mycobacterium tuberculosis enzyme is not.
A. K. ROOS, S. MARIANO, E. KOWALINSKI, L. SALMON, and S. L. MOWBRAY
J. Mol. Biol. 2008, 382, 667-679.

Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily.
S. J. J. BROUNS, T. R. M. BARENDS, P. WORM, J. AKERBOOM, A. P. TURNBULL, L. SALMON, and J. VAN DER OOST
J. Mol. Biol.
2008, 379, 357-371.

Binding of 5-phospho-D-arabinonohydroxamate and 5-phospho-D-arabinonate inhibitors to zinc phosphomannose isomerase from Candida albicans studied by polarizable molecular mechanics and quantum mechanics.
C. ROUX, N. GRESH, L. E. PERERA, J.-P. PIQUEMAL, and L. SALMON
J. Comput. Chem. 2007, 28, 938-957.

Ribose-5-phosphate isomerase type B from Trypanosoma cruzi: kinetic properties and site-directed mutagenesis reveal information about the reaction mechanism.
A. L. STERN, E. BURGOS, L. SALMON, and J.-J. CAZZULO
Biochem. J. 2007, 401, 279-285.

Identification of the missing links in the prokaryotic pentose oxidation pathway: evidence for enzyme recruitment.
S. J. J. BROUNS, J. WALTHER, A. P. L. SNIJDERS, H. J. G. VAN DE WERKEN, H. L. D. M. WILLEMEN, P. WORM, M. G. J. DE VOS, A. ANDERSSON, M. LUNDGREN, H. F. M. MAZON, R. H. H. VAN DEN HEUVEL, P. NILSSON, L. SALMON, W. M. DE VOS, P. C. WRIGHT, R. BERNANDER and J. VAN DER OOST
J. Biol. Chem. 2006, 281, 27378-27388.

Preliminary studies on the inhibition of D-sorbitol-6-phosphate 2-dehydrogenase from Escherichia coli with substrate analogues.
C. ROUX, L. SALMON, and C. VERCHÈRE-BÉAUR
J. Enzyme Inhib. Med. Chem. 2006, 21, 187-192.

Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism.
A. K. ROOS, E. BURGOS, D. J. ERICSSON, L. SALMON, and S. L. MOWBRAY
J. Biol. Chem. 2005, 280, 6416-6422.

Synthesis of 5-deoxy-5-phospho-D-ribonohydroxamic acid: a new competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosis.
E. BURGOS, A. K. ROOS, S. L. MOWBRAY, and L. SALMON
Tetrahedron Lett.
2005, 46, 3691-3694.

The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose Isomerase provide insights into substrate binding and catalysis.
J. M. BERRISFORD, J. AKERBOOM, S. BROUNS, S. E. SEDELNIKOVA, A. P. TURNBULL, J. VAN DER OOST, L. SALMON, R. HARDRÉ, I. A. MURRAY, G. M. BLACKBURN, D. W. RICE, and P. BAKER
J. Mol. Biol. 2004, 343, 649-657.

Leishmania mexicana mexicana glucose-6-phosphate isomerase crystallization, molecular replacement solution and inhibition.
A. T. CORDEIRO, R. HARDRÉ, P. A. M. MICHELS, L. SALMON, L. F. DELBONI, and O. H. THIEMANN
Acta. Crystallogr. 2004, D60, 915-919.

Synthesis and kinetic evaluation of 4-deoxy-4-phosphonomethyl-D-erythronate, the first hydrolytically stable and potent competitive inhibitor of ribose-5-phosphate isomerase.
E. BURGOS and L. SALMON
Tetrahedron Lett.
2004, 45, 3465-3469.

Synthesis and evaluation of new 4-phospho-D-erythronic acid derivatives as competitive inhibitors of spinach ribose-5-phosphate isomerase.
E. BURGOS and L. SALMON
Tetrahedron Lett.
2004, 45, 753-756.

Inhibition of type I and type II phosphomannose isomerases by the reaction intermediate analogue 5-phospho-D-arabinonohydroxamic acid supports a catalytic role for the metal cofactor.
C. ROUX, J. H. LEE, C. J. JEFFERY, and L. SALMON
Biochemistry
2004, 43, 2926-2934.

Sugar derivatives as new 6-phosphogluconate dehydrogenase inhibitors selective for the parasite Trypanosoma brucei.
C. PASTI, E. RINALDI, C. CERVELLATI, F. DALLOCCHIO, R. HARDRÉ, L. SALMON, and S. HANAU
Bioorg. Med. Chem.
2003, 11, 1207-1214.

The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid.
D. ARSENIEVA, R. HARDRÉ, L. SALMON, and C. J. JEFFERY
Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 5872-5877.

A convenient preparation of aldonohydroxamic acids in water and crystal structure of L-erythronohydroxamic acid.
L. SALMON, E. PROST, C. MERIENNE, R. HARDRÉ, and G. MORGANT
Carbohydr. Res.
2001, 335, 195-204.

The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
C. J. JEFFERY, R. HARDRÉ, and L. SALMON
Biochemistry 2001, 40, 1560-1566.


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