Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.
about
Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡Structures of type B ribose 5-phosphate isomerase from Trypanosoma cruzi shed light on the determinants of sugar specificity in the structural familyBinding Energy and Catalysis by d -Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of ( R )-GlyceraldehydeEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseConnecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymeReflections on the catalytic power of a TIM-barrel.Enzymatic Catalysis of Proton Transfer and Decarboxylation Reactions.α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.Activation of R235A mutant orotidine 5'-monophosphate decarboxylase by the guanidinium cation: effective molarity of the cationic side chain of Arg-235Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.Bovine serum albumin-catalyzed deprotonation of [1-(13)C]glycolaldehyde: protein reactivity toward deprotonation of the alpha-hydroxy alpha-carbonyl carbon.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate DecarboxylaseIsopentenyl diphosphate isomerase catalyzed reactions in D2O: product release limits the rate of this sluggish enzyme-catalyzed reaction.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.The importance of the leader sequence for directing lanthionine formation in lacticin 481.Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseDissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5'-phosphate decarboxylase-catalyzed reactions.A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase (NAD+) by phosphite dianion.Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organismsEnzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.Pyridoxal 5'-phosphate: electrophilic catalyst extraordinaire.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesA role for flexible loops in enzyme catalysis.The PLP cofactor: lessons from studies on model reactions.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Specificity in transition state binding: the Pauling model revisited.Enzyme activation through the utilization of intrinsic dianion binding energy.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.
P2860
Q27651151-6205DEB8-6640-4EED-89B3-96D4238ABDC6Q27666451-D6FE8F40-4C41-435D-BD5F-7E0CF49FBD0AQ27675003-0B931482-008A-43BB-82E3-493E7F424E97Q27683776-8A0EC762-DBA0-4179-9B4A-CEE9263F81F2Q27703607-2BAFAF7D-6BB4-4CB7-B659-406957CC7D24Q30365425-2433C050-E13E-41B1-B210-9210F872BB97Q30602492-65DD6B0D-208F-4291-99DD-43DFB2667E5DQ30841403-BCA33B63-CE47-40C4-A2D6-094AB2700B7CQ31141859-1B70FF3B-9E0A-470B-8923-37D011F7387DQ33641029-DC0155ED-7B67-4E90-A19B-3EAC05310277Q33893026-6C6FDC47-EEE1-4741-B779-17EC22AAD890Q33931303-7EC15FDB-908D-42CC-B8C8-83B6D41ECC33Q34101654-FD8F6206-F025-444A-981C-18645FCC4FC2Q34489862-02F88B42-BBE2-4AEB-B1B1-BCAD49F1E361Q34996638-31FF81F6-DA06-4C63-AAF9-8EAC86E4D303Q35031849-D6FF709F-6021-4BB1-B7F8-84CACB12677EQ35460625-E15CE70F-7062-4129-A2B1-84069F0D504AQ35560639-92CBD9F2-A06D-43B8-B962-F28AFA799A58Q35904170-3C9DD8C8-DB41-4601-A78F-9FBBA9D3ACEEQ35908467-67E66F1B-69BE-45E2-8453-FAE3F3FE6E50Q36049435-9C880390-EE66-4EF1-937F-148ECFE86B26Q36411077-EE59BF43-D267-4E23-AC8C-400E9392843CQ36953058-FFAFA425-E64E-4FA3-8334-785A982A0426Q37068901-017BCB05-2829-43C4-8092-F2B41E445945Q37120622-4B429CA2-B726-45C6-9F9B-B684B2A26368Q37208516-3AD13DC7-ACC9-41D6-B7C3-8444B6773F2CQ37337726-393A3FDC-D6AB-40A8-A0CB-29161F3C2042Q37363206-7616E4DE-3D12-4470-8FAE-92D97ED225B9Q37363849-250A80B4-F8E2-4A80-909E-1B1F525C1AF1Q37368445-A90BABE5-B17B-491E-85DF-7C83256F088DQ37503752-720045D7-6F8F-4271-BAF0-80CEF0B7DB80Q37565896-41148F09-687B-477D-AA3E-A6824E81FEF4Q37692215-079924CB-BF87-4F99-A7DE-B11BCE85750CQ37701676-6E77EF8B-AAB2-40AE-A881-5BDC2BBC0136Q37800559-B78B351C-5BFC-4C3E-B3A2-5C755289DEF0Q37823717-19879929-10AC-4AEA-B0AF-FE6A8A5B87FFQ37992670-FF4CD736-F7A6-4C83-A5BE-2233DA221F4AQ38074690-324881F4-0D84-48FB-8AF6-A0EBA032F943Q39024949-16EA48B0-FB27-41CB-9FFC-2CD054F84A45Q41246660-6BB70C81-3C8E-42C3-89A2-3C649C1D833B
P2860
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.
description
2007 nî lūn-bûn
@nan
2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@ast
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@en
type
label
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@ast
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@en
prefLabel
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@ast
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@en
P2860
P356
P1433
P1476
Enzymatic catalysis of proton ...... somerase by phosphite dianion.
@en
P2093
Tina L Amyes
P2860
P304
P356
10.1021/BI700409B
P407
P577
2007-04-20T00:00:00Z