M. J. Adams, G. H. Ellis, S. Gover, C. E. Naylor, and C. Phillips, Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism, Structure, vol.2, issue.7, pp.651-668, 1994.
DOI : 10.1016/S0969-2126(00)00066-6

S. Bailey, A. H. Fairlamb, and W. N. Hunter, Structure of trypanothione reductase from Crithidia fasciculata at 2.6 ?? resolution; enzyme???NADP interactions at 2.8 ?? resolution, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.2, pp.139-154, 1994.
DOI : 10.1107/S0907444993011898

P. J. Baker, K. L. Britton, D. W. Rice, A. Rob, and T. J. Stillman, Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold, Journal of Molecular Biology, vol.228, issue.2, pp.662-671, 1992.
DOI : 10.1016/0022-2836(92)90848-E

N. Bernard, K. Johnsen, J. J. Holbrook, and J. Delcour, D175 Discriminates Between NADH and NADPH in the Coenzyme Binding Site of Lactobacillus delbrueckii subsp. Bulgaricus D-Lactate Dehydrogenase, Biochemical and Biophysical Research Communications, vol.208, issue.3, pp.895-900, 1995.
DOI : 10.1006/bbrc.1995.1419

F. C. Bernstein, T. F. Koetzle, G. J. Williams, E. F. Meyer, . Jr et al., The protein data bank: A computer-based archival file for macromolecular structures, Journal of Molecular Biology, vol.112, issue.3, pp.535-542, 1977.
DOI : 10.1016/S0022-2836(77)80200-3

G. Biesecker, J. I. Harris, J. C. Thierry, J. E. Walker, and A. J. Wonacott, Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus, Nature, vol.69, issue.5600, pp.328-333, 1977.
DOI : 10.1042/bj1190805f

J. A. Bocanegra, N. S. Scrutton, and R. N. Perham, Creation of an NADP-dependent pyruvate dehydro- genase multienzyme complex by protein engineering, Biochemistry, vol.32, 1993.

J. T. Bolin, D. J. Filman, D. A. Matthews, R. C. Hamlin, and J. Kraut, Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase re®ned at 1.7 A Ê resolution. I. General features and binding of methotrexate, J. Biol. Chem, vol.257, 1982.

P. Bork and C. Grunwald, Recognition of different nucleotide-binding sites in primary structures using a property-pattern approach, European Journal of Biochemistry, vol.26, issue.2, pp.347-358, 1990.
DOI : 10.1038/343038a0

È. Bru and A. T. Nger, Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, vol.355, pp.472-475, 1992.

È. Bru and A. T. Nger, X-PLOR Manual, version 3, 1992.

È. Bru, A. T. Nger, J. Kuriyan, and M. Karplus, Crystallographic R-factor re®nement by molecular dynamics, Science, vol.229, pp.458-460, 1987.

M. Buehner, G. C. Ford, D. Moras, K. W. Olsen, and M. G. Rossmann, Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.90, issue.1, 1974.
DOI : 10.1016/0022-2836(74)90254-X

C. Bystroff, S. J. Oatley, and J. Kraut, Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state, Biochemistry, vol.29, issue.13, pp.3263-3277, 1990.
DOI : 10.1021/bi00465a018

R. Cerff, Glyceraldehyde-3-Phosphate Dehydrogenase(NADP) from Sinapis alba L.. NAD(P)-Induced Conformation Changes of the Enzyme, European Journal of Biochemistry, vol.87, issue.1, 1978.
DOI : 10.1016/0003-9861(64)90184-5

R. Cerff, Quaternary Structure of Higher Plant Glyceraldehyde-3-Phosphate Dehydrogenases, European Journal of Biochemistry, vol.61, issue.1, pp.243-247, 1979.
DOI : 10.1016/0003-9861(73)90064-7

P. Chakrabarti and U. Samanta, CH/?? Interaction in the Packing of the Adenine Ring in Protein Structures, Journal of Molecular Biology, vol.251, issue.1, pp.9-14, 1995.
DOI : 10.1006/jmbi.1995.0411

J. N. Champness, A. Achari, S. P. Ballantine, P. K. Bryant, C. J. Delves et al., The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 ?? resolution, Structure, vol.2, issue.10, pp.915-924, 1994.
DOI : 10.1016/S0969-2126(94)00093-X

R. Chen, A. Greer, and A. M. Dean, A highly active decarboxylating dehydrogenase with rationally inverted coenzyme speci®city, Proc. Natl Acad, 1995.

Z. Chen, W. R. Lee, and S. H. Chang, Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase, European Journal of Biochemistry, vol.24, issue.2, pp.263-267, 1991.
DOI : 10.1016/0167-4838(82)90125-X

S. Clermont, C. Corbier, Y. Mely, G. Ârard, D. Wonacott et al., Determinants of coenzyme speci®city in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the ®ngerprint region of the nucleotide binding fold, Biochemistry, vol.32, 1993.

V. Cody, J. R. Luft, E. Ciszak, T. I. Kalman, and J. H. Freisheim, Crystal structure determination at 2.3 A Ê of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-g-tetrazole . Anti-cancer Drug Des, pp.483-491, 1992.

C. Corbier, S. Clermont, P. Billard, T. Skarzynski, C. Branlant et al., Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis, Biochemistry, vol.29, issue.30, pp.7101-7106, 1990.
DOI : 10.1021/bi00482a022

URL : https://hal.archives-ouvertes.fr/hal-01652724

G. Branlant, The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis, Biochimie, pp.72-545, 1990.

D. Âe, E. Olivier-deyris, L. Fanchon, E. Corbier, C. Branlant et al., Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity, J. Mol. Biol, vol.257, pp.814-838, 1996.

O. El-kabbani, N. C. Green, G. Lin, M. Carson, S. V. Narayana et al., Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.6, pp.859-868, 1994.
DOI : 10.1107/S0907444994005275

O. El-kabbani, K. Judge, S. L. Ginell, D. A. Myles, L. J. Delucas et al., Structure of porcine aldehyde reductase holoenzyme, Nature Structural Biology, vol.4, issue.8, pp.687-692, 1995.
DOI : 10.1016/0168-9002(94)90720-X

R. A. Engh and R. Huber, Accurate bond and angle parameters for X-ray protein structure re®nement, Acta Crystallog. sect. A, pp.47-392, 1991.
DOI : 10.1107/s0108767391001071

URL : http://journals.iucr.org/a/issues/1991/04/00/li0061/li0061.pdf

F. Fan, J. A. Lorenzen, and B. V. Plapp, An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme, Biochemistry, vol.30, issue.26, pp.6397-6401, 1991.
DOI : 10.1021/bi00240a008

G. Ferri, G. Comerio, P. Iadarola, M. C. Zapponi, and M. L. Speranza, Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.522, issue.1, 1978.
DOI : 10.1016/0005-2744(78)90318-2

G. Ferri, M. Stoppini, M. L. Meloni, M. C. Zapponi, and P. Iadarola, Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1041, issue.1, pp.36-42, 1041.
DOI : 10.1016/0167-4838(90)90119-Z

D. J. Filman, J. T. Bolin, D. A. Matthews, and J. Kraut, Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase re®ned at 1.7 A Ê resolution. II. Environment of bound NADPH and implications for catalysis, J. Biol. Chem, vol.257, 1982.

I. Fita and M. G. Rossmann, The NADPH binding site on beef liver catalase., Proc. Natl Acad. Sci. USA, 1604.
DOI : 10.1073/pnas.82.6.1604

P. Gouet, H. Jouve, and O. Dideberg, Crystal Structure ofProteus mirabilisPR Catalase With and Without Bound NADPH, Journal of Molecular Biology, vol.249, issue.5, pp.933-954, 1995.
DOI : 10.1006/jmbi.1995.0350

C. E. Grimshaw, D. A. Matthews, K. I. Varughese, M. Skinner, N. H. Xuong et al., Characterization of nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37- isoleucine replacement, J. Biol. Chem, vol.267, 1992.

L. Haeffner-gormley, Z. Chen, H. Zalkin, and R. F. Colman, Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium, Biochemistry, vol.31, issue.34, pp.31-7807, 1992.
DOI : 10.1021/bi00149a010

I. Hanukoglu and T. Gut®nger, cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases, European Journal of Biochemistry, vol.14, issue.2, pp.479-484, 1989.
DOI : 10.1146/annurev.biophys.15.1.321

E. T. Harper and G. D. Rose, Helix stop signals in proteins and peptides: The capping box, Biochemistry, vol.32, issue.30, pp.7605-7609, 1993.
DOI : 10.1021/bi00081a001

J. I. Harris and M. Waters, Glyceraldehyde-3-phos- phate dehydrogenase, The Enzymes, pp.1-49, 1976.

S. S. Hoog, J. E. Pawlowski, P. M. Alzari, T. M. Penning, and M. Lewis, Three-dimensional structure of rat liver 3a-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily, Proc. Natl Acad. Sci. USA, 91, 1994.

S. Huang, J. R. Appleman, X. Tan, P. D. Thompson, R. L. Blakley et al., Role of lysine-54 in determining cofactor specificity and binding in human dihydrofolate reductase, Biochemistry, vol.29, issue.35, pp.8063-8069, 1990.
DOI : 10.1021/bi00487a011

J. H. Hurley and A. M. Dean, Structure of 3???isopropylmalate dehydrogenase in complex with NAD+: ligand???induced loop closing and mechanism for cofactor specificity, Structure, vol.2, issue.11, pp.1007-1016, 1994.
DOI : 10.1016/S0969-2126(94)00104-9

J. H. Hurley, A. M. Dean, D. E. Koshland, &. Jr, and R. M. Stroud, Catalytic mechanism of NADP+-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes, Biochemistry, vol.30, issue.35, pp.8671-8678, 1991.
DOI : 10.1021/bi00099a026

W. Kabsch, Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector, Journal of Applied Crystallography, vol.21, issue.6, 1988.
DOI : 10.1107/S0021889888007903

W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, Journal of Applied Crystallography, vol.26, issue.6, pp.795-800, 1993.
DOI : 10.1107/S0021889893005588

H. Kim, I. K. Feil, C. L. Verlinde, P. H. Petra, and W. G. Hol, Crystal Structure of Glycosomal Glyceraldehyde-3-phosphate Dehydrogenase from Leishmania mexicana: Implications for Structure-Based Drug Design and a New Position for the Inorganic Phosphate Binding Site, Biochemistry, vol.34, issue.46, pp.14975-14986, 1995.
DOI : 10.1021/bi00046a004

È. Korndo, I. Rfer, B. Steipe, R. Huber, A. Tomschy et al., The Crystal Structure of Holo-glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic BacteriumThermotoga maritimaat 2.5 ?? Resolution, Journal of Molecular Biology, vol.246, issue.4, pp.511-521, 1995.
DOI : 10.1006/jmbi.1994.0103

P. J. Kraulis, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991.
DOI : 10.1107/S0021889891004399

V. Lauvergeat, K. Kennedy, C. Feuillet, J. H. Mckie, L. Gorrichon et al., Site-directed mutagenesis of a serine residue in cinnamyl alcohol dehydrogenase, a plant NADPH-dependent dehydrogenase , affects the speci®city for the coenzyme, Biochemistry, vol.34, 1995.

A. M. Lesk, NAD-binding domains of dehydrogenases, Current Opinion in Structural Biology, vol.5, issue.6, pp.775-783, 1995.
DOI : 10.1016/0959-440X(95)80010-7

A. G. Leslie and A. J. Wonacott, Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.165, issue.2, pp.375-391, 1983.
DOI : 10.1016/S0022-2836(83)80262-9

N. Interactions, H. R. Levy, V. E. Vought, X. Yin, and M. J. Adams, Identi®cation of an arginine residue in the dual coenzyme-speci®c glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides that plays a key role in binding NADP ‡ but not NAD ‡, Arch. Biochem. Biophys, vol.326, pp.145-151, 1996.

Z. Lin, J. Li, F. Zhang, S. Song, J. Yang et al., Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase from Palinurus versicolor Carrying the Fluorescent NAD Derivatives at 2.7?? Resolution, Archives of Biochemistry and Biophysics, vol.302, issue.1, pp.161-166, 1993.
DOI : 10.1006/abbi.1993.1194

W. Martin and R. Cerff, Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phos- phate dehydrogenases from mustard, 1986.

F. S. Mathews, New flavoenzymes, Current Opinion in Structural Biology, vol.1, issue.6, pp.954-967, 1991.
DOI : 10.1016/0959-440X(91)90091-7

M. A. Mctigue, J. F. Davies, . Ii, B. T. Kaufman, and J. Kraut, Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin, Biochemistry, vol.31, issue.32, pp.31-7264, 1992.
DOI : 10.1021/bi00147a009

W. D. Mercer, S. I. Winn, and H. C. Watson, Twinning in crystals of human skeletal muscle d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.104, issue.1, pp.277-283, 1976.
DOI : 10.1016/0022-2836(76)90013-9

M. H. Metzger and C. P. Hollenberg, Amino Acid Substitutions in the Yeast Pichia Stipitis Xylitol Dehydrogenase Coenzyme-Binding Domain Affect the Coenzyme Specificity, European Journal of Biochemistry, vol.187, issue.1, pp.50-54, 1995.
DOI : 10.1038/343038a0

P. R. Mittl and G. E. Schulz, Structure of glutathione reductase from escherichia coli at 1.86 ?? resolution: Comparison with the enzyme from human erythrocytes, Protein Science, vol.250, issue.5, pp.799-809, 1994.
DOI : 10.1042/bj2450875

P. R. Mittl, A. Berry, N. S. Scrutton, R. N. Perham, and G. E. Schulz, Anatomy of an engineered NAD-binding site, Protein Science, vol.187, issue.9, 1504.
DOI : 10.1042/bj2450875

K. Miyazaki and T. Oshima, HB8, "Protein Engineering, Design and Selection", vol.7, issue.3, pp.401-403, 1994.
DOI : 10.1093/protein/7.3.401

D. Moras, K. W. Olsen, M. N. Sabesan, M. Buehner, G. C. Ford et al., Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.250, pp.9137-9162, 1975.

A. Mougin, C. Corbier, A. Soukri, A. Wonacott, C. Branlant et al., in the formation of charge-transfer transition in glyceraldehyde-3-phosphate dehydrogenase, "Protein Engineering, Design and Selection", vol.2, issue.1, pp.45-48, 1988.
DOI : 10.1093/protein/2.1.45

M. Nishiyama, J. J. Birktoft, and T. Beppu, Alteration of coenzyme speci®city of malate dehydrogenase from Thermus ¯avus by site-directed mutagenesis, J. Biol. Chem, vol.268, pp.4656-4660, 1993.

Z. Otwinowski, Oscillation data reduction program, Proceedings of the CCP4 Study Weekend: Data Collection and Processing, pp.56-62, 1993.

E. F. Pai, Variations on a theme: the family of FAD-dependent NAD(P)H-(disulphide)-oxidoreductases, Current Opinion in Structural Biology, vol.1, issue.5, pp.796-803, 1991.
DOI : 10.1016/0959-440X(91)90181-R

E. Racker and I. Krimsky, The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.198, pp.731-743, 1952.

S. Rahuel-clermont, Etude des facteurs mole Âculaires responsables de la spe Âci®cite  de cofacteur des de Âshydroge Ânases a Á NAD(P). The Áse d, 1994.

M. G. Rossmann, M. J. Adams, M. Buehner, G. C. Ford, M. L. Hackert et al., Molecular symmetry axes and subunit interfaces in certain dehydrogenases, Journal of Molecular Biology, vol.76, issue.4, pp.533-537, 1973.
DOI : 10.1016/0022-2836(73)90491-9

M. G. Rossmann, D. Moras, and K. W. Olsen, Chemical and biological evolution of a nucleotide-binding protein, Nature, vol.243, issue.5463, pp.194-199, 1974.
DOI : 10.1101/SQB.1972.036.01.032

M. G. Rossmann, A. Liljas, È. Bra, C. Nde-Ân, and L. J. Banaszak, 2 Evolutionary and Structural Relationships among Dehydrogenases, The Enzymes, pp.61-102, 1975.
DOI : 10.1016/S1874-6047(08)60210-3

A. Roussel and C. Cambillau, TURBO-FRODO, Silicon Graphics Geometry Partner Directory (Silicon graphics, pp.77-78, 1989.

G. E. Schulz, Binding of nucleotides by proteins, Current Opinion in Structural Biology, vol.2, issue.1, pp.61-67, 1992.
DOI : 10.1016/0959-440X(92)90178-A

N. S. Scrutton, A. Berry, and R. N. Perham, Redesign of the coenzyme specificity of a dehydrogenase by protein engineering, Nature, vol.343, issue.6253, pp.38-43, 1990.
DOI : 10.1038/343038a0

J. W. Seale, R. Srinivasan, and G. D. Rose, Sequence determinants of the capping box, a stabilizing motif at the N-termini of ??-helices, Protein Science, vol.31, issue.10, 1741.
DOI : 10.1111/j.1399-3011.1993.tb00470.x

D. S. Sem and C. B. Kasper, Enzyme-substrate binding interactions of NADPH-cytochrome P-450 oxidoreductase characterized with pH and alternate substrate/inhibitor studies, Biochemistry, vol.32, issue.43, pp.11539-11547, 1993.
DOI : 10.1021/bi00094a010

D. S. Sem and C. B. Kasper, Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH, Biochemistry, vol.32, issue.43, 1993.
DOI : 10.1021/bi00094a011

M. Shih, G. Lazar, and H. M. Goodman, Evidence in favor of the symbiotic origin of chloroplasts: Primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenases, Cell, vol.47, issue.1, pp.47-73, 1986.
DOI : 10.1016/0092-8674(86)90367-3

T. Skarzynski and A. J. Wonacott, Coenzymeinduced conformational changes in glyceraldehyde- 3-phosphate dehydrogenase from Bacillus stearothermophilus, J. Mol. Biol, vol.203, 1097.

T. Skarzynski, P. C. Moody, and A. J. Wonacott, Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 ?? resolution, Journal of Molecular Biology, vol.193, issue.1, pp.171-187, 1987.
DOI : 10.1016/0022-2836(87)90635-8

B. L. Stoddard, A. Dean, D. E. Koshland, and . Jr, Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-.ANG. resolution: A pseudo-Michaelis ternary complex, Biochemistry, vol.32, issue.36, pp.9310-9316, 1993.
DOI : 10.1021/bi00087a008

N. Interactions, M. Sundaralingam, and Y. C. Sekharudu, Waterinserted a-helical segments implicate reverse turns as folding intermediates, Science, vol.244, pp.1333-1337, 1989.

J. J. Tanner, R. M. Hecht, and K. L. Krause, Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceral- dehyde-3-phosphate dehydrogenase at 2.5 A Ê resolution, Biochemistry, vol.35, 1996.

J. A. Thomas, J. R. Arnold, J. Basran, J. Andrews, G. C. Roberts et al., dihydrofolate reductase, "Protein Engineering, Design and Selection", vol.7, issue.6, pp.783-792, 1994.
DOI : 10.1093/protein/7.6.783

J. M. Thorn, J. D. Barton, N. E. Dixon, D. L. Ollis, and K. J. Edwards, Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed with NADPH, Journal of Molecular Biology, vol.249, issue.4, pp.785-799, 1995.
DOI : 10.1006/jmbi.1995.0337

H. C. Watson, E. Due-Âe, and W. D. Mercer, Low Resolution Structure of Glyceraldehyde 3-Phosphate Dehydrogenase, Nature New Biology, vol.240, issue.100, pp.130-139, 1972.
DOI : 10.1038/newbio240130a0

R. K. Wierenga, P. Terpstra, and W. G. Hol, Prediction of the occurrence of the ADP-binding ??????-fold in proteins, using an amino acid sequence fingerprint, Journal of Molecular Biology, vol.187, issue.1, pp.101-107, 1986.
DOI : 10.1016/0022-2836(86)90409-2

D. K. Wilson, K. M. Bohren, K. H. Gabbay, and F. A. Quiocho, An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications, Science, vol.257, issue.5066, pp.81-84, 1992.
DOI : 10.1126/science.1621098

T. Yaoi, K. Miyazaki, and T. Oshima, isocitrate dehydrogenase in the coenzyme specificity, FEBS Letters, vol.221, issue.2, pp.171-172, 1994.
DOI : 10.1111/j.1432-1033.1994.tb18805.x