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
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
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
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
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
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
Creation of an NADP-dependent pyruvate dehydro- genase multienzyme complex by protein engineering, Biochemistry, vol.32, 1993. ,
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. ,
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
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, vol.355, pp.472-475, 1992. ,
X-PLOR Manual, version 3, 1992. ,
Crystallographic R-factor re®nement by molecular dynamics, Science, vol.229, pp.458-460, 1987. ,
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
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
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
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
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
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
A highly active decarboxylating dehydrogenase with rationally inverted coenzyme speci®city, Proc. Natl Acad, 1995. ,
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
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. ,
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. ,
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
The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis, Biochimie, pp.72-545, 1990. ,
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. ,
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
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
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
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
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
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
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. ,
The NADPH binding site on beef liver catalase., Proc. Natl Acad. Sci. USA, 1604. ,
DOI : 10.1073/pnas.82.6.1604
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
Characterization of nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37- isoleucine replacement, J. Biol. Chem, vol.267, 1992. ,
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
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
Helix stop signals in proteins and peptides: The capping box, Biochemistry, vol.32, issue.30, pp.7605-7609, 1993. ,
DOI : 10.1021/bi00081a001
Glyceraldehyde-3-phos- phate dehydrogenase, The Enzymes, pp.1-49, 1976. ,
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. ,
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
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
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
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
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
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
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
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
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. ,
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
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
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. ,
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
Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phos- phate dehydrogenases from mustard, 1986. ,
New flavoenzymes, Current Opinion in Structural Biology, vol.1, issue.6, pp.954-967, 1991. ,
DOI : 10.1016/0959-440X(91)90091-7
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
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
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
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
Anatomy of an engineered NAD-binding site, Protein Science, vol.187, issue.9, 1504. ,
DOI : 10.1042/bj2450875
HB8, "Protein Engineering, Design and Selection", vol.7, issue.3, pp.401-403, 1994. ,
DOI : 10.1093/protein/7.3.401
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.250, pp.9137-9162, 1975. ,
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
Alteration of coenzyme speci®city of malate dehydrogenase from Thermus ¯avus by site-directed mutagenesis, J. Biol. Chem, vol.268, pp.4656-4660, 1993. ,
Oscillation data reduction program, Proceedings of the CCP4 Study Weekend: Data Collection and Processing, pp.56-62, 1993. ,
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
The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.198, pp.731-743, 1952. ,
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. ,
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
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
2 Evolutionary and Structural Relationships among Dehydrogenases, The Enzymes, pp.61-102, 1975. ,
DOI : 10.1016/S1874-6047(08)60210-3
TURBO-FRODO, Silicon Graphics Geometry Partner Directory (Silicon graphics, pp.77-78, 1989. ,
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
Redesign of the coenzyme specificity of a dehydrogenase by protein
engineering, Nature, vol.343, issue.6253, pp.38-43, 1990. ,
DOI : 10.1038/343038a0
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
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
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
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
Coenzymeinduced conformational changes in glyceraldehyde- 3-phosphate dehydrogenase from Bacillus stearothermophilus, J. Mol. Biol, vol.203, 1097. ,
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
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
Waterinserted a-helical segments implicate reverse turns as folding intermediates, Science, vol.244, pp.1333-1337, 1989. ,
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. ,
dihydrofolate reductase, "Protein Engineering, Design and Selection", vol.7, issue.6, pp.783-792, 1994. ,
DOI : 10.1093/protein/7.6.783
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
Low Resolution Structure of Glyceraldehyde 3-Phosphate Dehydrogenase, Nature New Biology, vol.240, issue.100, pp.130-139, 1972. ,
DOI : 10.1038/newbio240130a0
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
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
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