(en) W. John Albery et Jeremy R. Knowles, « Free-energy profile for the reaction catalyzed by triosephosphate isomerase », Biochemistry, vol. 15, no 25, , p. 5627-5631 (PMID999838, DOI10.1021/bi00670a031, lire en ligne)
(en) Irwin A. Rose, Wen Jian Fung et Jessie V. B. Warms, « Proton diffusion in the active site of triosephosphate isomerase », Biochemistry, vol. 29, no 18, , p. 4312-4317 (PMID2161683, DOI10.1021/bi00470a008, lire en ligne)
(en) Patricia J. Lodi, Louise C. Chang, Jeremy R. Knowles et Elizabeth A. Komives, « Triosephosphate Isomerase Requires a Positively Charged Active Site: The Role of Lysine-12 », Biochemistry, vol. 33, no 10, , p. 2809-2814 (PMID8130193, DOI10.1021/bi00176a009, lire en ligne)
(en) Elliott B. Nickbarg, Robert C. Davenport, Gregory A. Petsko et Jeremy R. Knowles, « Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism », Biochemistry, vol. 27, no 16, , p. 5948-5960 (PMID2847777, DOI10.1021/bi00416a019, lire en ligne)
(en) Elizabeth A. Komives, Louise C. Chang, Elias Lolis, Robert F. Tilton, Gregory A. Petsko et Jeremy R. Knowles, « Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95 », Biochemistry, vol. 30, no 12, , p. 3011-3019 (PMID2007138, DOI10.1021/bi00226a005, lire en ligne)
(en) Thomas K. Harris, Robert N. Cole, Frank I. Comer et Albert S. Mildvan, « Proton Transfer in the Mechanism of Triosephosphate Isomerase », Biochemistry, vol. 37, no 47, , p. 16828-16838 (PMID9843453, DOI10.1021/bi982089f, lire en ligne)
(en) Elias Lolis et Gregory A. Petsko, « Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: implications for catalysis », Biochemistry, vol. 29, no 28, , p. 6619-6625 (PMID2204418, DOI10.1021/bi00480a010, lire en ligne)
doi.org
dx.doi.org
(en) T. Kinoshita, R. Maruki, M. Warizaya, H. Nakajima et S. Nishimura, « Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method », Acta Crystallographica Section F, vol. 61, no Pt 4, , p. 346-349 (PMID16511037, PMCID1952429, DOI10.1107/S1744309105008341, lire en ligne)
(en) W. John Albery et Jeremy R. Knowles, « Free-energy profile for the reaction catalyzed by triosephosphate isomerase », Biochemistry, vol. 15, no 25, , p. 5627-5631 (PMID999838, DOI10.1021/bi00670a031, lire en ligne)
(en) Irwin A. Rose, Wen Jian Fung et Jessie V. B. Warms, « Proton diffusion in the active site of triosephosphate isomerase », Biochemistry, vol. 29, no 18, , p. 4312-4317 (PMID2161683, DOI10.1021/bi00470a008, lire en ligne)
(en) Donald J. Creighton et Diana S. Hamilton, « Brief History of Glyoxalase I and What We Have Learned about Metal Ion-Dependent, Enzyme-Catalyzed Isomerizations », Archives of Biochemistry and Biophysics, vol. 387, no 1, , p. 1-10 (PMID11368170, DOI10.1006/abbi.2000.2253, lire en ligne)
(en) Patricia J. Lodi, Louise C. Chang, Jeremy R. Knowles et Elizabeth A. Komives, « Triosephosphate Isomerase Requires a Positively Charged Active Site: The Role of Lysine-12 », Biochemistry, vol. 33, no 10, , p. 2809-2814 (PMID8130193, DOI10.1021/bi00176a009, lire en ligne)
(en) T. Alber, D. W. Banner, A. C. Bloomer, G. A. Petsko, David Phillips, P. S. Rivers et I. A. Wilson, « On the Three-Dimensional Structure and Catalytic Mechanism of Triose Phosphate Isomerase », Philosophical Transactions B, vol. 293, no 1063, , p. 159-171 (PMID6115415, DOI10.1098/rstb.1981.0069, lire en ligne)
(en) Elliott B. Nickbarg, Robert C. Davenport, Gregory A. Petsko et Jeremy R. Knowles, « Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism », Biochemistry, vol. 27, no 16, , p. 5948-5960 (PMID2847777, DOI10.1021/bi00416a019, lire en ligne)
(en) Elizabeth A. Komives, Louise C. Chang, Elias Lolis, Robert F. Tilton, Gregory A. Petsko et Jeremy R. Knowles, « Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95 », Biochemistry, vol. 30, no 12, , p. 3011-3019 (PMID2007138, DOI10.1021/bi00226a005, lire en ligne)
(en) Thomas K. Harris, Robert N. Cole, Frank I. Comer et Albert S. Mildvan, « Proton Transfer in the Mechanism of Triosephosphate Isomerase », Biochemistry, vol. 37, no 47, , p. 16828-16838 (PMID9843453, DOI10.1021/bi982089f, lire en ligne)
(en) Anne-Marie Lambeir, Fred R. Opperdoes et Rik K. Wierenga, « Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei », The FEBS Journal, vol. 168, no 1, , p. 69-74 (PMID3311744, DOI10.1111/j.1432-1033.1987.tb13388.x, lire en ligne)
(en) Elias Lolis et Gregory A. Petsko, « Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: implications for catalysis », Biochemistry, vol. 29, no 28, , p. 6619-6625 (PMID2204418, DOI10.1021/bi00480a010, lire en ligne)
iucr.org
scripts.iucr.org
(en) T. Kinoshita, R. Maruki, M. Warizaya, H. Nakajima et S. Nishimura, « Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method », Acta Crystallographica Section F, vol. 61, no Pt 4, , p. 346-349 (PMID16511037, PMCID1952429, DOI10.1107/S1744309105008341, lire en ligne)
(en) T. Kinoshita, R. Maruki, M. Warizaya, H. Nakajima et S. Nishimura, « Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method », Acta Crystallographica Section F, vol. 61, no Pt 4, , p. 346-349 (PMID16511037, PMCID1952429, DOI10.1107/S1744309105008341, lire en ligne)
(en) W. John Albery et Jeremy R. Knowles, « Free-energy profile for the reaction catalyzed by triosephosphate isomerase », Biochemistry, vol. 15, no 25, , p. 5627-5631 (PMID999838, DOI10.1021/bi00670a031, lire en ligne)
(en) Irwin A. Rose, Wen Jian Fung et Jessie V. B. Warms, « Proton diffusion in the active site of triosephosphate isomerase », Biochemistry, vol. 29, no 18, , p. 4312-4317 (PMID2161683, DOI10.1021/bi00470a008, lire en ligne)
(en) Donald J. Creighton et Diana S. Hamilton, « Brief History of Glyoxalase I and What We Have Learned about Metal Ion-Dependent, Enzyme-Catalyzed Isomerizations », Archives of Biochemistry and Biophysics, vol. 387, no 1, , p. 1-10 (PMID11368170, DOI10.1006/abbi.2000.2253, lire en ligne)
(en) Patricia J. Lodi, Louise C. Chang, Jeremy R. Knowles et Elizabeth A. Komives, « Triosephosphate Isomerase Requires a Positively Charged Active Site: The Role of Lysine-12 », Biochemistry, vol. 33, no 10, , p. 2809-2814 (PMID8130193, DOI10.1021/bi00176a009, lire en ligne)
(en) T. Alber, D. W. Banner, A. C. Bloomer, G. A. Petsko, David Phillips, P. S. Rivers et I. A. Wilson, « On the Three-Dimensional Structure and Catalytic Mechanism of Triose Phosphate Isomerase », Philosophical Transactions B, vol. 293, no 1063, , p. 159-171 (PMID6115415, DOI10.1098/rstb.1981.0069, lire en ligne)
(en) Elliott B. Nickbarg, Robert C. Davenport, Gregory A. Petsko et Jeremy R. Knowles, « Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism », Biochemistry, vol. 27, no 16, , p. 5948-5960 (PMID2847777, DOI10.1021/bi00416a019, lire en ligne)
(en) Elizabeth A. Komives, Louise C. Chang, Elias Lolis, Robert F. Tilton, Gregory A. Petsko et Jeremy R. Knowles, « Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95 », Biochemistry, vol. 30, no 12, , p. 3011-3019 (PMID2007138, DOI10.1021/bi00226a005, lire en ligne)
(en) Thomas K. Harris, Robert N. Cole, Frank I. Comer et Albert S. Mildvan, « Proton Transfer in the Mechanism of Triosephosphate Isomerase », Biochemistry, vol. 37, no 47, , p. 16828-16838 (PMID9843453, DOI10.1021/bi982089f, lire en ligne)
(en) Anne-Marie Lambeir, Fred R. Opperdoes et Rik K. Wierenga, « Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei », The FEBS Journal, vol. 168, no 1, , p. 69-74 (PMID3311744, DOI10.1111/j.1432-1033.1987.tb13388.x, lire en ligne)
(en) Elias Lolis et Gregory A. Petsko, « Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-Å resolution: implications for catalysis », Biochemistry, vol. 29, no 28, , p. 6619-6625 (PMID2204418, DOI10.1021/bi00480a010, lire en ligne)
royalsocietypublishing.org
rstb.royalsocietypublishing.org
(en) T. Alber, D. W. Banner, A. C. Bloomer, G. A. Petsko, David Phillips, P. S. Rivers et I. A. Wilson, « On the Three-Dimensional Structure and Catalytic Mechanism of Triose Phosphate Isomerase », Philosophical Transactions B, vol. 293, no 1063, , p. 159-171 (PMID6115415, DOI10.1098/rstb.1981.0069, lire en ligne)
sciencedirect.com
(en) Donald J. Creighton et Diana S. Hamilton, « Brief History of Glyoxalase I and What We Have Learned about Metal Ion-Dependent, Enzyme-Catalyzed Isomerizations », Archives of Biochemistry and Biophysics, vol. 387, no 1, , p. 1-10 (PMID11368170, DOI10.1006/abbi.2000.2253, lire en ligne)
(en) Anne-Marie Lambeir, Fred R. Opperdoes et Rik K. Wierenga, « Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei », The FEBS Journal, vol. 168, no 1, , p. 69-74 (PMID3311744, DOI10.1111/j.1432-1033.1987.tb13388.x, lire en ligne)