-
1
-
-
0000283648
-
Perfection in enzyme catalysis: The energetics of triosephosphate isomerase
-
Knowles, J. R. and Albery, W. J. (1977) Perfection in enzyme catalysis: The energetics of triosephosphate isomerase Acc. Chem. Res. 10, 105-111
-
(1977)
Acc. Chem. Res.
, vol.10
, pp. 105-111
-
-
Knowles, J.R.1
Albery, W.J.2
-
3
-
-
0014941582
-
Uniquely labeled active site sequence in chicken muscle triosephosphate isomerase
-
Coulson, A. F. W., Knowles, J. R., Priddle, J. D., and Offord, R. E. (1970) Uniquely labeled active site sequence in chicken muscle triosephosphate isomerase Nature 227, 180-181
-
(1970)
Nature
, vol.227
, pp. 180-181
-
-
Coulson, A.F.W.1
Knowles, J.R.2
Priddle, J.D.3
Offord, R.E.4
-
4
-
-
0014936667
-
Isolation and characterization of an active-site peptide from triosephosphate isomerase
-
Hartman, F. C. (1970) Isolation and characterization of an active-site peptide from triosephosphate isomerase J. Am. Chem. Soc. 92, 2170-2172
-
(1970)
J. Am. Chem. Soc.
, vol.92
, pp. 2170-2172
-
-
Hartman, F.C.1
-
5
-
-
36949045756
-
Identification of site in triosephosphate isomerase labeled by glycidol phosphate
-
Waley, S. G., Miller, J. C., Rose, I. A., and O'Connell, E. L. (1970) Identification of site in triosephosphate isomerase labeled by glycidol phosphate Nature 227, 181
-
(1970)
Nature
, vol.227
, pp. 181
-
-
Waley, S.G.1
Miller, J.C.2
Rose, I.A.3
O'Connell, E.L.4
-
6
-
-
0028279839
-
Crystal Structure of the Mutant Yeast Triosephosphate Isomerase in Which the Catalytic Base Glutamic Acid 165 Is Changed to Aspartic Acid
-
Joseph-McCarthy, D., Rost, L. E., Komives, E. A., and Petsko, G. A. (1994) Crystal Structure of the Mutant Yeast Triosephosphate Isomerase in Which the Catalytic Base Glutamic Acid 165 Is Changed to Aspartic Acid Biochemistry 33, 2824-2829
-
(1994)
Biochemistry
, vol.33
, pp. 2824-2829
-
-
Joseph-Mccarthy, D.1
Rost, L.E.2
Komives, E.A.3
Petsko, G.A.4
-
7
-
-
0025871717
-
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: Structural origins and catalytic implications
-
Lodi, P. J. and Knowles, J. R. (1991) Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: Structural origins and catalytic implications Biochemistry 30, 6948-6956
-
(1991)
Biochemistry
, vol.30
, pp. 6948-6956
-
-
Lodi, P.J.1
Knowles, J.R.2
-
8
-
-
0025893928
-
Electrophilic catalysis in triosephosphate isomerase: The role of histidine-95
-
Komives, E. A., Chang, L. C., Lolis, E., Tilton, R. F., Petsko, G. A., and Knowles, J. R. (1991) Electrophilic catalysis in triosephosphate isomerase: The role of histidine-95 Biochemistry 30, 3011-3019
-
(1991)
Biochemistry
, vol.30
, pp. 3011-3019
-
-
Komives, E.A.1
Chang, L.C.2
Lolis, E.3
Tilton, R.F.4
Petsko, G.A.5
Knowles, J.R.6
-
9
-
-
0024282745
-
Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
-
Nickbarg, E. B., Davenport, R. C., Petsko, G. A., and Knowles, J. R. (1988) Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism Biochemistry 27, 5948-5960
-
(1988)
Biochemistry
, vol.27
, pp. 5948-5960
-
-
Nickbarg, E.B.1
Davenport, R.C.2
Petsko, G.A.3
Knowles, J.R.4
-
10
-
-
0027133903
-
An Explanation for Rapid Enzyme-Catalyzed Proton Abstraction from Carbon Acids: Importance of Late Transition States in Concerted Mechanisms
-
Gerlt, J. A. and Gassman, P. G. (1993) An Explanation for Rapid Enzyme-Catalyzed Proton Abstraction from Carbon Acids: Importance of Late Transition States in Concerted Mechanisms J. Am. Chem. Soc. 115, 11552-11568
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 11552-11568
-
-
Gerlt, J.A.1
Gassman, P.G.2
-
12
-
-
70449257873
-
Mechanism of the triosephosphate isomerase reaction
-
Rieder, S. V. and Rose, I. A. (1959) Mechanism of the triosephosphate isomerase reaction J. Biol. Chem. 234, 1007-1010
-
(1959)
J. Biol. Chem.
, vol.234
, pp. 1007-1010
-
-
Rieder, S.V.1
Rose, I.A.2
-
15
-
-
0025763437
-
Enzyme catalysis: Not different, just better
-
Knowles, J. R. (1991) Enzyme catalysis: Not different, just better Nature 350, 121-124
-
(1991)
Nature
, vol.350
, pp. 121-124
-
-
Knowles, J.R.1
-
16
-
-
77953888039
-
Role of Lys-12 in Catalysis by Triosephosphate Isomerase: A Two-Part Substrate Approach
-
Go, M. K., Koudelka, A., Amyes, T. L., and Richard, J. P. (2010) Role of Lys-12 in Catalysis by Triosephosphate Isomerase: A Two-Part Substrate Approach Biochemistry 49, 5377-5389
-
(2010)
Biochemistry
, vol.49
, pp. 5377-5389
-
-
Go, M.K.1
Koudelka, A.2
Amyes, T.L.3
Richard, J.P.4
-
17
-
-
77957104394
-
Rescue of K12G Triosephosphate Isomerase by Ammonium Cations: The Reaction of an Enzyme in Pieces
-
Go, M. K., Amyes, T. L., and Richard, J. P. (2010) Rescue of K12G Triosephosphate Isomerase by Ammonium Cations: The Reaction of an Enzyme in Pieces J. Am. Chem. Soc. 132, 13525-13532
-
(2010)
J. Am. Chem. Soc.
, vol.132
, pp. 13525-13532
-
-
Go, M.K.1
Amyes, T.L.2
Richard, J.P.3
-
18
-
-
84859417694
-
A Paradigm for Enzyme-Catalyzed Proton Transfer at Carbon: Triosephosphate Isomerase
-
Richard, J. P. (2012) A Paradigm for Enzyme-Catalyzed Proton Transfer at Carbon: Triosephosphate Isomerase Biochemistry 51, 2652-2661
-
(2012)
Biochemistry
, vol.51
, pp. 2652-2661
-
-
Richard, J.P.1
-
19
-
-
84876742875
-
Magnitude and Origin of the Enhanced Basicity of the Catalytic Glutamate of Triosephosphate Isomerase
-
Malabanan, M. M., Nitsch-Velasquez, L., Amyes, T. L., and Richard, J. P. (2013) Magnitude and Origin of the Enhanced Basicity of the Catalytic Glutamate of Triosephosphate Isomerase J. Am. Chem. Soc. 135, 5978-5981
-
(2013)
J. Am. Chem. Soc.
, vol.135
, pp. 5978-5981
-
-
Malabanan, M.M.1
Nitsch-Velasquez, L.2
Amyes, T.L.3
Richard, J.P.4
-
20
-
-
84862563121
-
Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Hydrophobic Clamp
-
Malabanan, M. M., Koudelka, A. P., Amyes, T. L., and Richard, J. P. (2012) Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Hydrophobic Clamp J. Am. Chem. Soc. 134, 10286-10298
-
(2012)
J. Am. Chem. Soc.
, vol.134
, pp. 10286-10298
-
-
Malabanan, M.M.1
Koudelka, A.P.2
Amyes, T.L.3
Richard, J.P.4
-
21
-
-
80054730874
-
Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Ligand-Driven Conformational Change
-
Malabanan, M. M., Amyes, T. L., and Richard, J. P. (2011) Mechanism for Activation of Triosephosphate Isomerase by Phosphite Dianion: The Role of a Ligand-Driven Conformational Change J. Am. Chem. Soc. 133, 16428-16431
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 16428-16431
-
-
Malabanan, M.M.1
Amyes, T.L.2
Richard, J.P.3
-
22
-
-
0025276041
-
Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
-
Pompliano, D. L., Peyman, A., and Knowles, J. R. (1990) Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase Biochemistry 29, 3186-3194
-
(1990)
Biochemistry
, vol.29
, pp. 3186-3194
-
-
Pompliano, D.L.1
Peyman, A.2
Knowles, J.R.3
-
23
-
-
0026779802
-
Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase
-
Sampson, N. S. and Knowles, J. R. (1992) Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase Biochemistry 31, 8482-8487
-
(1992)
Biochemistry
, vol.31
, pp. 8482-8487
-
-
Sampson, N.S.1
Knowles, J.R.2
-
24
-
-
0026782489
-
Segmental motion in catalysis: Investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase
-
Sampson, N. S. and Knowles, J. R. (1992) Segmental motion in catalysis: Investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase Biochemistry 31, 8488-8494
-
(1992)
Biochemistry
, vol.31
, pp. 8488-8494
-
-
Sampson, N.S.1
Knowles, J.R.2
-
25
-
-
4444321214
-
Entropy effects on protein hinges: The reaction catalyzed by triosephosphate isomerase
-
Xiang, J., Jung, J.-y., and Sampson, N. S. (2004) Entropy effects on protein hinges: The reaction catalyzed by triosephosphate isomerase Biochemistry 43, 11436-11445
-
(2004)
Biochemistry
, vol.43
, pp. 11436-11445
-
-
Xiang, J.1
Jung, J.2
Sampson, N.S.3
-
26
-
-
0035815109
-
The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase
-
Xiang, J., Sun, J., and Sampson, N. S. (2001) The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase J. Mol. Biol. 307, 1103-1112
-
(2001)
J. Mol. Biol.
, vol.307
, pp. 1103-1112
-
-
Xiang, J.1
Sun, J.2
Sampson, N.S.3
-
27
-
-
78649649414
-
A role for flexible loops in enzyme catalysis
-
Malabanan, M. M., Amyes Tina, L., and Richard John, P. (2010) A role for flexible loops in enzyme catalysis Curr. Opin. Struct. Biol. 20, 702-710
-
(2010)
Curr. Opin. Struct. Biol.
, vol.20
, pp. 702-710
-
-
Malabanan, M.M.1
Amyes Tina, L.2
Richard John, P.3
-
28
-
-
66349134420
-
Role of Loop-Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase
-
Wang, Y., Berlow, R. B., and Loria, J. P. (2009) Role of Loop-Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase Biochemistry 48, 4548-4556
-
(2009)
Biochemistry
, vol.48
, pp. 4548-4556
-
-
Wang, Y.1
Berlow, R.B.2
Loria, J.P.3
-
29
-
-
4143134253
-
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
-
Kursula, I., Salin, M., Sun, J., Norledge, B. V., Haapalainen, A. M., Sampson, N. S., and Wierenga, R. K. (2004) Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase Protein Eng., Des. Sel. 17, 375-382
-
(2004)
Protein Eng., Des. Sel.
, vol.17
, pp. 375-382
-
-
Kursula, I.1
Salin, M.2
Sun, J.3
Norledge, B.V.4
Haapalainen, A.M.5
Sampson, N.S.6
Wierenga, R.K.7
-
30
-
-
34248548552
-
Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite Dianion
-
Amyes, T. L. and Richard, J. P. (2007) Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite Dianion Biochemistry 46, 5841-5854
-
(2007)
Biochemistry
, vol.46
, pp. 5841-5854
-
-
Amyes, T.L.1
Richard, J.P.2
-
31
-
-
27844574242
-
Activation of orotidine 5′-monophosphate decarboxylase by phosphite dianion: The whole substrate is the sum of two parts
-
Amyes, T. L., Richard, J. P., and Tait, J. J. (2005) Activation of orotidine 5′-monophosphate decarboxylase by phosphite dianion: The whole substrate is the sum of two parts J. Am. Chem. Soc. 127, 15708-15709
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 15708-15709
-
-
Amyes, T.L.1
Richard, J.P.2
Tait, J.J.3
-
32
-
-
79955438648
-
OMP Decarboxylase: Phosphodianion Binding Energy Is Used to Stabilize a Vinyl Carbanion Intermediate
-
Goryanova, B., Amyes, T. L., Gerlt, J. A., and Richard, J. P. (2011) OMP Decarboxylase: Phosphodianion Binding Energy Is Used To Stabilize a Vinyl Carbanion Intermediate J. Am. Chem. Soc. 133, 6545-6548
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 6545-6548
-
-
Goryanova, B.1
Amyes, T.L.2
Gerlt, J.A.3
Richard, J.P.4
-
35
-
-
0017173701
-
An analysis of the substrate-induced rate effect in the phosphoglucomutase system
-
Ray, W. J., Jr., Long, J. W., and Owens, J. D. (1976) An analysis of the substrate-induced rate effect in the phosphoglucomutase system Biochemistry 15, 4006-4017
-
(1976)
Biochemistry
, vol.15
, pp. 4006-4017
-
-
Ray, Jr.W.J.1
Long, J.W.2
Owens, J.D.3
-
36
-
-
84875780747
-
DXP Reductoisomerase: Reaction of the Substrate in Pieces Reveals a Catalytic Role for the Nonreacting Phosphodianion Group
-
Kholodar, S. A. and Murkin, A. S. (2013) DXP Reductoisomerase: Reaction of the Substrate in Pieces Reveals a Catalytic Role for the Nonreacting Phosphodianion Group Biochemistry 52, 2302-2308
-
(2013)
Biochemistry
, vol.52
, pp. 2302-2308
-
-
Kholodar, S.A.1
Murkin, A.S.2
-
37
-
-
84875636822
-
Specificity in Transition State Binding: The Pauling Model Revisited
-
Amyes, T. L. and Richard, J. P. (2013) Specificity in Transition State Binding: The Pauling Model Revisited Biochemistry 52, 2021-2035
-
(2013)
Biochemistry
, vol.52
, pp. 2021-2035
-
-
Amyes, T.L.1
Richard, J.P.2
-
38
-
-
0016624901
-
Binding Energy, Specificity and Enzymic Catalysis: The Circe Effect
-
Jencks, W. P. (1975) Binding Energy, Specificity and Enzymic Catalysis: The Circe Effect Adv. Enzymol. Relat. Areas Mol. Biol. 43, 219-410
-
(1975)
Adv. Enzymol. Relat. Areas Mol. Biol.
, vol.43
, pp. 219-410
-
-
Jencks, W.P.1
-
39
-
-
0041866694
-
Mapping Chemical Exchange in Proteins with MW > 50 kD
-
Wang, C., Rance, M., and Palmer, A. G. (2003) Mapping Chemical Exchange in Proteins with MW > 50 kD J. Am. Chem. Soc. 125, 8968-8969
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 8968-8969
-
-
Wang, C.1
Rance, M.2
Palmer, A.G.3
-
40
-
-
33745642439
-
Off-Resonance TROSY-Selected R1ρ Experiment with Improved Sensitivity for Medium- and High-Molecular-Weight Proteins
-
Igumenova, T. I. and Palmer, A. G. (2006) Off-Resonance TROSY-Selected R1ρ Experiment with Improved Sensitivity for Medium- and High-Molecular-Weight Proteins J. Am. Chem. Soc. 128, 8110-8111
-
(2006)
J. Am. Chem. Soc.
, vol.128
, pp. 8110-8111
-
-
Igumenova, T.I.1
Palmer, A.G.2
-
41
-
-
33845964234
-
Functional role of the conserved active site proline of triosephosphate isomerase
-
Casteleijn, M. G., Alahuhta, M., Groebel, K., El-Sayed, I., Augustyns, K., Lambeir, A.-M., Neubauer, P., and Wierenga, R. K. (2006) Functional role of the conserved active site proline of triosephosphate isomerase Biochemistry 45, 15483-15494
-
(2006)
Biochemistry
, vol.45
, pp. 15483-15494
-
-
Casteleijn, M.G.1
Alahuhta, M.2
Groebel, K.3
El-Sayed, I.4
Augustyns, K.5
Lambeir, A.-M.6
Neubauer, P.7
Wierenga, R.K.8
-
43
-
-
48649103139
-
A Metabolic Bypass of the Triosephosphate Isomerase Reaction
-
Desai, K. K. and Miller, B. G. (2008) A Metabolic Bypass of the Triosephosphate Isomerase Reaction Biochemistry 47, 7983-7985
-
(2008)
Biochemistry
, vol.47
, pp. 7983-7985
-
-
Desai, K.K.1
Miller, B.G.2
-
44
-
-
0033621030
-
Understanding Protein Lids: Kinetic Analysis of Active Hinge Mutants in Triosephosphate Isomerase
-
Sun, J. and Sampson, N. S. (1999) Understanding Protein Lids: Kinetic Analysis of Active Hinge Mutants in Triosephosphate Isomerase Biochemistry 38, 11474-11481
-
(1999)
Biochemistry
, vol.38
, pp. 11474-11481
-
-
Sun, J.1
Sampson, N.S.2
-
45
-
-
27144505097
-
Protein identification and analysis tools on the ExPASy server
-
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., and Bairoch, A. (2005) Protein identification and analysis tools on the ExPASy server Proteomics Protoc. Handb. 571-607
-
(2005)
Proteomics Protoc. Handb.
, pp. 571-607
-
-
Gasteiger, E.1
Hoogland, C.2
Gattiker, A.3
Duvaud, S.4
Wilkins, M.R.5
Appel, R.D.6
Bairoch, A.7
-
46
-
-
0043122944
-
ExPASy: The proteomics server for in-depth protein knowledge and analysis
-
Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R. D., and Bairoch, A. (2003) ExPASy: The proteomics server for in-depth protein knowledge and analysis Nucleic Acids Res. 31, 3784-3788
-
(2003)
Nucleic Acids Res.
, vol.31
, pp. 3784-3788
-
-
Gasteiger, E.1
Gattiker, A.2
Hoogland, C.3
Ivanyi, I.4
Appel, R.D.5
Bairoch, A.6
-
47
-
-
0027401730
-
Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterization of a dimer-interface mutant
-
Borchert, T. V., Pratt, K., Zeelen, J. P., Callens, M., Noble, M. E. M., Opperdoes, F. R., Michels, P. A. M., and Wierenga, R. K. (1993) Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterization of a dimer-interface mutant Eur. J. Biochem. 211, 703-710
-
(1993)
Eur. J. Biochem.
, vol.211
, pp. 703-710
-
-
Borchert, T.V.1
Pratt, K.2
Zeelen, J.P.3
Callens, M.4
Noble, M.E.M.5
Opperdoes, F.R.6
Michels, P.A.M.7
Wierenga, R.K.8
-
48
-
-
6444222991
-
Use of glass electrodes to measure acidities in deuterium oxide
-
Glasoe, P. K. and Long, F. A. (1960) Use of glass electrodes to measure acidities in deuterium oxide J. Phys. Chem. 64, 188-190
-
(1960)
J. Phys. Chem.
, vol.64
, pp. 188-190
-
-
Glasoe, P.K.1
Long, F.A.2
-
50
-
-
0015394088
-
PH-Dependence of the triosephosphate isomerase reaction
-
Plaut, B. and Knowles, J. R. (1972) pH-Dependence of the triosephosphate isomerase reaction Biochem. J. 129, 311-320
-
(1972)
Biochem. J.
, vol.129
, pp. 311-320
-
-
Plaut, B.1
Knowles, J.R.2
-
51
-
-
0030567338
-
a of Ethyl Acetate: Brønsted Correlation for Deprotonation of a Simple Oxygen Ester in Aqueous Solution
-
a of Ethyl Acetate: Brønsted Correlation for Deprotonation of a Simple Oxygen Ester in Aqueous Solution J. Am. Chem. Soc. 118, 3129-3141
-
(1996)
J. Am. Chem. Soc.
, vol.118
, pp. 3129-3141
-
-
Amyes, T.L.1
Richard, J.P.2
-
52
-
-
0000047442
-
Generation and stability of a simple thiol ester enolate in aqueous solution
-
Amyes, T. L. and Richard, J. P. (1992) Generation and stability of a simple thiol ester enolate in aqueous solution J. Am. Chem. Soc. 114, 10297-10302
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 10297-10302
-
-
Amyes, T.L.1
Richard, J.P.2
-
53
-
-
77956136607
-
13C]- Glycolaldehyde: Protein Reactivity toward Deprotonation of α-Hydroxy α-Carbonyl Carbon
-
13C]- Glycolaldehyde: Protein Reactivity toward Deprotonation of α-Hydroxy α-Carbonyl Carbon Biochemistry 49, 7704-7708
-
(2010)
Biochemistry
, vol.49
, pp. 7704-7708
-
-
Go, M.K.1
Malabanan, M.M.2
Amyes, T.L.3
Richard, J.P.4
-
55
-
-
0022483315
-
Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties
-
Misset, O., Bos, O. J., and Opperdoes, F. R. (1986) Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties Eur. J. Biochem. 157, 441-453
-
(1986)
Eur. J. Biochem.
, vol.157
, pp. 441-453
-
-
Misset, O.1
Bos, O.J.2
Opperdoes, F.R.3
-
56
-
-
0026519169
-
Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase
-
Wierenga, R. K., Noble, M. E. M., and Davenport, R. C. (1992) Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase J. Mol. Biol. 224, 1115-1126
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 1115-1126
-
-
Wierenga, R.K.1
Noble, M.E.M.2
Davenport, R.C.3
-
57
-
-
77953514501
-
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: New insight in the proton transfer reaction mechanism
-
Alahuhta, M. and Wierenga, R. K. (2010) Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: New insight in the proton transfer reaction mechanism Proteins: Struct., Funct., Bioinf. 78, 1878-1888
-
(2010)
Proteins: Struct., Funct., Bioinf.
, vol.78
, pp. 1878-1888
-
-
Alahuhta, M.1
Wierenga, R.K.2
-
58
-
-
0028209049
-
Crystal Structure of Recombinant Chicken Triosephosphate Isomerase-Phosphoglycolohydroxamate Complex at 1.8-Å Resolution
-
Zhang, Z., Sugio, S., Komives, E. A., Liu, K. D., Knowles, J. R., Petsko, G. A., and Ringe, D. (1994) Crystal Structure of Recombinant Chicken Triosephosphate Isomerase-Phosphoglycolohydroxamate Complex at 1.8-Å Resolution Biochemistry 33, 2830-2837
-
(1994)
Biochemistry
, vol.33
, pp. 2830-2837
-
-
Zhang, Z.1
Sugio, S.2
Komives, E.A.3
Liu, K.D.4
Knowles, J.R.5
Petsko, G.A.6
Ringe, D.7
-
59
-
-
78651330006
-
Triosephosphate isomerase: A highly evolved biocatalyst
-
Wierenga, R. K., Kapetaniou, E. G., and Venkatesan, R. (2010) Triosephosphate isomerase: A highly evolved biocatalyst Cell. Mol. Life Sci. 67, 3961-3982
-
(2010)
Cell. Mol. Life Sci.
, vol.67
, pp. 3961-3982
-
-
Wierenga, R.K.1
Kapetaniou, E.G.2
Venkatesan, R.3
-
60
-
-
0015394032
-
Specificity and kinetics of triosephosphate isomerase from chicken muscle
-
Putman, S. J., Coulson, A. F. W., Farley, I. R. T., Riddleston, B., and Knowles, J. R. (1972) Specificity and kinetics of triosephosphate isomerase from chicken muscle Biochem. J. 129, 301-310
-
(1972)
Biochem. J.
, vol.129
, pp. 301-310
-
-
Putman, S.J.1
Coulson, A.F.W.2
Farley, I.R.T.3
Riddleston, B.4
Knowles, J.R.5
-
62
-
-
0002903441
-
Analog approaches to the structure of the transition state in enzyme reactions
-
Wolfenden, R. (1972) Analog approaches to the structure of the transition state in enzyme reactions Acc. Chem. Res. 5, 10-18
-
(1972)
Acc. Chem. Res.
, vol.5
, pp. 10-18
-
-
Wolfenden, R.1
-
63
-
-
0014681301
-
Transition state analogues for enzyme catalysis
-
Wolfenden, R. (1969) Transition state analogues for enzyme catalysis Nature 223, 704-705
-
(1969)
Nature
, vol.223
, pp. 704-705
-
-
Wolfenden, R.1
-
64
-
-
84872763037
-
Catalysis by Orotidine 5′-Monophosphate Decarboxylase: Effect of 5-Fluoro and 4′-Substituents on the Decarboxylation of Two-Part Substrates
-
Goryanova, B., Spong, K., Amyes, T. L., and Richard, J. P. (2013) Catalysis by Orotidine 5′-Monophosphate Decarboxylase: Effect of 5-Fluoro and 4′-Substituents on the Decarboxylation of Two-Part Substrates Biochemistry 52, 537-546
-
(2013)
Biochemistry
, vol.52
, pp. 537-546
-
-
Goryanova, B.1
Spong, K.2
Amyes, T.L.3
Richard, J.P.4
-
65
-
-
84862196265
-
Orotidine 5′-monophosphate decarboxylase: Transition state stabilization from remote protein-phosphodianion interactions
-
Amyes, T. L., Ming, S. A., Goldman, L. M., Wood, B. M., Desai, B. J., Gerlt, J. A., and Richard, J. P. (2012) Orotidine 5′-monophosphate decarboxylase: Transition state stabilization from remote protein-phosphodianion interactions Biochemistry 51, 4630-4632
-
(2012)
Biochemistry
, vol.51
, pp. 4630-4632
-
-
Amyes, T.L.1
Ming, S.A.2
Goldman, L.M.3
Wood, B.M.4
Desai, B.J.5
Gerlt, J.A.6
Richard, J.P.7
-
66
-
-
48249090425
-
Dissecting the Total Transition State Stabilization Provided by Amino Acid Side Chains at Orotidine 5′-Monophosphate Decarboxylase: A Two-Part Substrate Approach
-
Barnett, S. A., Amyes, T. L., Wood, B. M., Gerlt, J. A., and Richard, J. P. (2008) Dissecting the Total Transition State Stabilization Provided by Amino Acid Side Chains at Orotidine 5′-Monophosphate Decarboxylase: A Two-Part Substrate Approach Biochemistry 47, 7785-7787
-
(2008)
Biochemistry
, vol.47
, pp. 7785-7787
-
-
Barnett, S.A.1
Amyes, T.L.2
Wood, B.M.3
Gerlt, J.A.4
Richard, J.P.5
-
67
-
-
75749143420
-
Activation of R235A Mutant Orotidine 5′-Monophosphate Decarboxylase by the Guanidinium Cation: Effective Molarity of the Cationic Side Chain of Arg-235
-
Barnett, S. A., Amyes, T. L., McKay, W. B., Gerlt, J. A., and Richard, J. P. (2010) Activation of R235A Mutant Orotidine 5′-Monophosphate Decarboxylase by the Guanidinium Cation: Effective Molarity of the Cationic Side Chain of Arg-235 Biochemistry 49, 824-826
-
(2010)
Biochemistry
, vol.49
, pp. 824-826
-
-
Barnett, S.A.1
Amyes, T.L.2
McKay, W.B.3
Gerlt, J.A.4
Richard, J.P.5
-
68
-
-
0019407381
-
On the attribution and additivity of binding energies
-
Jencks, W. P. (1981) On the attribution and additivity of binding energies Proc. Natl. Acad. Sci. U.S.A. 78, 4046-4050
-
(1981)
Proc. Natl. Acad. Sci. U.S.A.
, vol.78
, pp. 4046-4050
-
-
Jencks, W.P.1
-
69
-
-
0027242141
-
Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
-
Noble, M. E., Zeelen, J. P., and Wierenga, R. K. (1993) Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism Proteins 16, 311-326
-
(1993)
Proteins
, vol.16
, pp. 311-326
-
-
Noble, M.E.1
Zeelen, J.P.2
Wierenga, R.K.3
-
70
-
-
0037984337
-
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83 Å resolution
-
Kursula, I. and Wierenga, R. K. (2003) Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83 Å resolution J. Biol. Chem. 278, 9544-9551
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 9544-9551
-
-
Kursula, I.1
Wierenga, R.K.2
-
71
-
-
0037422593
-
Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution
-
Jogl, G., Rozovsky, S., McDermott, A. E., and Tong, L. (2003) Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution Proc. Natl. Acad. Sci. U.S.A. 100, 50-55
-
(2003)
Proc. Natl. Acad. Sci. U.S.A.
, vol.100
, pp. 50-55
-
-
Jogl, G.1
Rozovsky, S.2
McDermott, A.E.3
Tong, L.4
-
72
-
-
84962448531
-
The planar conformation of a strained proline ring: A QM/MM study
-
Donnini, S., Groenhof, G., Wierenga, R. K., and Juffer, A. H. (2006) The planar conformation of a strained proline ring: A QM/MM study Proteins 64, 700-710
-
(2006)
Proteins
, vol.64
, pp. 700-710
-
-
Donnini, S.1
Groenhof, G.2
Wierenga, R.K.3
Juffer, A.H.4
|