Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase
S Rozovsky, AE McDermott - Proceedings of the National …, 2007 - National Acad Sciences
The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol …
Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase
DL Pompliano, A Peyman, JR Knowles - Biochemistry, 1990 - ACS Publications
David L. Pompliano, 1 Anusch Peyman, 5 and Jeremy R. Knowles** Department of
Chemistry, Harvard University, Cambridge, Massachusetts 02138 Received September 15 …
Chemistry, Harvard University, Cambridge, Massachusetts 02138 Received September 15 …
Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
EB Nickbarg, RC Davenport, GA Petsko… - Biochemistry, 1988 - ACS Publications
Revised Manuscript Received March 21, 1988 abstract: An important active-siteresidue in
the glycolytic enzyme triosephosphate isomerase is His-95, which appears to act as an …
the glycolytic enzyme triosephosphate isomerase is His-95, which appears to act as an …
Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product
SG Maister, CP Pett, WJ Albery, JR Knowles - Biochemistry, 1976 - ACS Publications
Selwyn G. Maister, Christopher P. Pett, W. John Albery,! and Jeremy R. Knowles** abstract:
When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is …
When the isomerization of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate is …
Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in product
SJ Fletcher, JM Herlihy, WJ Albery, JR Knowles - Biochemistry, 1976 - ACS Publications
Susan J. Fletcher, Julia M. Herlihy, W. John Albery, 1 and Jeremy R. Knowles* abstract:
When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is …
When the isomerization of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate is …
How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases
SC Blacklow, JR Knowles - Biochemistry, 1990 - ACS Publications
Stephen C. Blacklow and Jeremy R. Knowles* Department of Chemistry, Harvard University,
Cambridge, Massachusetts 02138 Received October 24, 1989; Revised Manuscript …
Cambridge, Massachusetts 02138 Received October 24, 1989; Revised Manuscript …
Liberation of the triosephosphate isomerase reaction intermediate and its trapping by isomerase, yeast aldolase, and methylglyoxal synthase
R Iyengar, IA Rose - Biochemistry, 1981 - ACS Publications
Radha Iyengar and Irwin A. Rose* abstract: When a mixture of triosephosphate isomerase
(rabbit muscle) and dihydroxyacetone phosphate (DHAP) is quenched with acid, a …
(rabbit muscle) and dihydroxyacetone phosphate (DHAP) is quenched with acid, a …
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications
PJ Lodi, JR Knowles - Biochemistry, 1991 - ACS Publications
To illuminate the role of histidine-95 in the catalytic reaction mediated by triosephosphate
isomerase, 13C and 15N NMR titration studies have been carried out both on the wild-type …
isomerase, 13C and 15N NMR titration studies have been carried out both on the wild-type …
Specificity and kinetics of triose phosphate isomerase from chicken muscle
SJ Putman, AFW Coulson, IRT Farley… - Biochemical …, 1972 - portlandpress.com
The isolation of crystalline triose phosphate isomerase from chicken breast muscle is
described. The values of k cat. and Km for the reaction in each direction were determined …
described. The values of k cat. and Km for the reaction in each direction were determined …
Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase
NS Sampson, JR Knowles - Biochemistry, 1992 - ACS Publications
Revised Manuscript Received May 28, 1992 abstract: A residue essential for proper closure
of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine …
of the active-site loop in the reaction catalyzed by triosephosphate isomerase is tyrosine …
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