The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
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pH Dependence of Catalysis by Pseudomonas aeruginosa Isochorismate–Pyruvate Lyase: Implications for Transition State Stabilization and the Role of Lysine 42Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issuesThe near attack conformation approach to the study of the chorismate to prephenate reaction.Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB.Pericyclic reactions catalyzed by chorismate-utilizing enzymes.Interdomain Conformational Changes Provide Allosteric Regulation En Route To ChorismateMechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complexMethyltransferases do not work by compression, cratic, or desolvation effects, but by electrostatic preorganization.Methodology Development in Directed Evolution: Exploring Options when Applying Triple-Code Saturation Mutagenesis.
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Q27670775-FE81C2AE-A4B7-4327-A398-B8A2AF425D5FQ30608426-69E6B1A1-0A77-42AE-BD52-DD9353A87267Q33917537-085235E6-DB36-4DDD-972B-2E461886F283Q34267037-F473272D-F131-4487-887D-1B221E90E001Q34299237-DC27E077-7408-47E6-93CE-82BA581691A0Q35184901-14DFD2F9-87AA-4990-A2E2-8C009A445F0BQ35188494-D7157F33-74D7-4F58-B99D-97431E82CA87Q39511364-CD770337-DD9D-41A1-87C6-8FBFA7DFB021Q39812909-0A541E65-92B3-43A9-AAC2-B167E268B4E5Q42027813-66867F8E-8726-4982-B18B-D1FA94CF54A3Q42183669-5A350BCD-C9ED-49EC-9775-426BDF120115Q48286865-DB9EBE40-8AA1-48C0-A059-C8CD1CE855F5
P2860
The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
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2002 nî lūn-bûn
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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2002 թվականի հունվարին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@ast
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@en
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@nl
type
label
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@ast
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@en
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@nl
prefLabel
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@ast
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@en
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@nl
P2860
P356
P1476
The mechanism of catalysis of ...... scherichia coli mutase enzyme.
@en
P2093
Thomas C Bruice
P2860
P304
P356
10.1073/PNAS.022628599
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P577
2002-01-29T00:00:00Z