Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach. - Wikidata - awgldk - TriplyDB

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

http://www.wikidata.org/entity/Q33931303

about

Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue Binding Energy and Catalysis by d -Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of ( R )-Glyceraldehyde Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate Isomerase Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme The heat released during catalytic turnover enhances the diffusion of an enzyme.Reflections on the catalytic power of a TIM-barrel.Structural effects of protein aging: terminal marking by deamidation in human triosephosphate isomerase.Enzymatic Catalysis of Proton Transfer and Decarboxylation Reactions.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.Bovine serum albumin-catalyzed deprotonation of [1-(13)C]glycolaldehyde: protein reactivity toward deprotonation of the alpha-hydroxy alpha-carbonyl carbon.Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces.Stabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.Common enzymological experiments allow free energy profile determination.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clamp Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride Transfer Evidence of a triosephosphate isomerase non-catalytic function crucial to behavior and longevity Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.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 pieces A role for flexible loops in enzyme catalysis.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Specificity in transition state binding: the Pauling model revisited.Enzyme architecture: on the importance of being in a protein cage.Enzyme activation through the utilization of intrinsic dianion binding energy.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.Characterization of stress and methylglyoxal inducible triose phosphate isomerase (OscTPI) from rice.A novel inhibitor of Mammalian triosephosphate isomerase found by an in silico approach.Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii.Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer.Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer.Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate Dehydrogenase Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase

P2860

Q27667142-9D1278DA-525B-410A-B60A-C6AA5E701487 Q27670430-EBEED498-8B60-49CA-A331-35AD4554F03D Q27675003-4606FE5B-D825-445D-BD3F-7E4E89D4410E Q27683517-EFE066A7-11B5-4D57-845D-BF4D187C0FDD Q27683776-526A859F-266E-459B-BABD-8F2105D9E52C Q27703607-9ADB738D-8E52-418C-BBFD-30A7A544A940 Q29302786-3E60DE12-AA20-423C-904C-0EE1915B81FA Q30365425-76A1D5E7-CBB7-4846-9B4B-488A41C9C7D0 Q30373836-1EE9F404-B70F-4F87-A94C-B03092C2E072 Q30602492-40967C16-7E72-411C-BCC2-E7AE1350956F Q33893026-CFC15C75-28EB-421C-B6E3-B88A0A6C9A43 Q34101654-E349F307-1155-41F7-8C18-141FE9CB25FB Q34154092-BC27585D-C6F9-4CA5-AF7D-8F19B97B6123 Q34255270-106B6B6F-F710-4535-9962-F0A8CDE61839 Q34859679-287C5FBA-594D-47D1-A625-600DD8BC6007 Q35031849-1591C742-8CCE-48F2-A558-C1106E82369D Q35560639-E0176108-C30B-411D-B335-295B721B18FA Q36049435-3F0040A0-0B41-4C76-89F0-946395BC2D21 Q36411077-B3E18EC1-2089-4E11-A1A3-0591D0C815ED Q36742403-7D851D9E-76E4-4040-8FE4-C2A85A0CEFC3 Q37012024-F043F23A-54CE-4CD6-8198-59BD4E84E348 Q37068901-C90FF6DB-8D7E-4F62-8FF6-B35455166EA3 Q37208516-7394E756-2869-4CBC-8BD7-FE8C78FCA4F7 Q37692215-DECA392D-208F-4328-A200-0C51B0207AF4 Q37701676-42599444-0CA3-4B85-96C3-057F112A3F45 Q37800559-EF284EA0-A316-4217-819D-2736F073032F Q37992670-FF396E6C-889A-4C1A-B07F-5EF31A22C41E Q38074690-8CA57EEA-D555-4AD3-8A1C-CCEA39FAB5C5 Q38201978-7EBE3A45-16AE-4E00-8329-49B6AEB1E7BA Q39024949-85183654-F0EE-4AD0-B616-83D3DFA52A74 Q39221322-0C9907AA-97EA-4D3F-87E5-2748B973A596 Q41246660-B4049560-40F8-41F7-9ED2-5AD10488C000 Q41335123-9BFD7FEC-29E4-4A92-BF00-E3EC5CEE9FAC Q41827899-0201F43E-3263-45DE-BCB0-85662288076D Q43031789-559BB414-192F-490A-A520-F27E0F4495B9 Q43102411-EFB1EAB0-A16B-4F2C-B141-F23AE529A44E Q48042720-B9B7D116-30AA-464B-9699-0CE451D73B43 Q57879771-E9196F79-414F-4265-9FE8-A57A4A228876 Q57879780-A5CEC983-3909-42CF-8471-0AB86455D500

P2860

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

http://www.wikidata.org/entity/Q33931303

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@ast

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@en

type

label

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@ast

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@en

prefLabel

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@ast

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@en

P1433

Q33931303-336ABEC7-7BB4-4B4D-8019-EDAB67029EAF

P1476

Q33931303-24E88FEA-45E4-445F-ACBC-ECB5A7058328

P2093

Q33931303-12FDD0B6-89B6-4E0F-BE58-45549CE453E6

Q33931303-980A1E7E-8BD0-4421-B3FB-5D5DF8D280AC

Q33931303-DC2F1BD2-4E35-45D5-9CCA-D160DF91E395

P2860

Q33931303-04077642-51BC-45A1-9A5B-8DB0C973BEEE

Q33931303-04283760-6DD0-4262-9DDE-56B1E5EE6EEB

Q33931303-27A529CD-82EF-4E0B-ADF4-65F47C99E2E1

Q33931303-2A9381D4-F961-4373-AD78-8816147C1F70

Q33931303-2BF7787E-01E5-4610-AAC4-67A3A85A3829

Q33931303-32551166-DA6C-4D14-B663-DBAF516A6AF1

Q33931303-3B584528-DAB5-4CF5-868A-5A6C768E6FCF

Q33931303-418E3A5B-1001-49B8-A694-F996E52F7651

Q33931303-42E35054-5B16-4888-9E70-1AF11FA6B884

Q33931303-47C60A31-6476-475A-A465-85787B766202

P304

Q33931303-331FE674-C1A1-4590-9B6C-7B44DF1F4988

P31

Q33931303-EFECAED4-3CD1-4C11-9143-1018F1862C08

P356

Q33931303-DE0A7547-27C5-4893-9F07-EB4570980DE1

P407

Q33931303-923939A3-00C2-49F6-9A87-84197CA31FCA

P433

Q33931303-28544340-0C6A-4133-8EB1-DFAA36C3DB8C

P478

Q33931303-BAC3AA59-966E-473E-9222-041249964E34

P50

Q33931303-C65CCF37-FCC4-4822-B00C-F24A089D7C89

P577

Q33931303-3796D452-B0BE-47B4-AFFE-24345FBA35E5

P5875

Q33931303-94780FEC-C2DE-41BC-B767-82C8A8A24817

P698

Q33931303-9747B358-6C85-4871-9E16-85D2DF8B8BBD

P932

Q33931303-B8A300F3-6147-4444-AF1D-BA9CCEDA6147

P356

P1433

P1476

Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.

@en

P2093

Astrid Koudelka

http://www.w3.org/2001/XMLSchema#string

Maybelle K Go

http://www.w3.org/2001/XMLSchema#string

Tina L Amyes

http://www.w3.org/2001/XMLSchema#string

P2860

On the attribution and additivity of binding energies

ExPASy: The proteomics server for in-depth protein knowledge and analysis

Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.

Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis

Triosephosphate isomerase: a theoretical comparison of alternative pathways

Triosephosphate isomerase requires a positively charged active site: the role of lysine-12

Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase

P304

5377-5389

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI100538B

http://www.w3.org/2001/XMLSchema#string

P407

P433

25

http://www.w3.org/2001/XMLSchema#string

P478

49

http://www.w3.org/2001/XMLSchema#string

P50

John P. Richard

P577

2010-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

44610326

http://www.w3.org/2001/XMLSchema#string

P698

20481463

http://www.w3.org/2001/XMLSchema#string

P932

2890037

http://www.w3.org/2001/XMLSchema#string