Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters.
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Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion holeIdentification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginineAn atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthasePosttranslational amino acid epimerization: enzyme-catalyzed isomerization of amino acid residues in peptide chainsKinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosisOn the electronic nature of low-barrier hydrogen bonds in enzymatic reactionsCrystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilizationAlternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexesStructural determinants for ligand binding and catalysis of triosephosphate isomeraseThe crystal structure of pectate lyase Pel9A from Erwinia chrysanthemiStructure of Mandelate Racemase with Bound Intermediate Analogues Benzohydroxamate and CupferronEvolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolaseBiochemical characterization of the chondroitinase B active siteIdentification of a catalytic aspartyl residue of D-ribulose 5-phosphate 3-epimerase by site-directed mutagenesisQM/MM calculations suggest a novel intermediate following the proton abstraction catalyzed by thymidylate synthaseEnzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site.Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase.Wildtype 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.Interaction of substrate uridyl 3',5'-adenosine with ribonuclease A: a molecular dynamics study.Catalytic reaction mechanism of acetylcholinesterase determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.Functional characteristics of the oxyanion hole in human acetylcholinesterase.The isomerization of Δ5-androstene-3,17-dione by the human glutathione transferase A3-3 proceeds via a conjugated heteroannular diene intermediateTransient intermediates in enzymology, 1964-2008.Contribution of a low-barrier hydrogen bond to catalysis is not significant in ketosteroid isomerase.Catalytic role of enzymes: short strong H-bond-induced partial proton shuttles and charge redistributions.Role of a critical water in scytalone dehydratase-catalyzed reaction.Non-enzymatic and enzymatic hydrolysis of alkyl halides: a haloalkane dehalogenation enzyme evolved to stabilize the gas-phase transition state of an SN2 displacement reactionOn the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates.Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMRThe change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis.Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseHydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by Thermoplasma acidophilum citrate synthaseThe Catalytic Mechanism of the Marine-Derived Macrocyclase PatGmacAcceleration of an aromatic Claisen rearrangement via a designed spiroligozyme catalyst that mimics the ketosteroid isomerase catalytic dyad.Why nature really chose phosphate.Biogenesis of D-amino acid containing peptides/proteins: where, when and how?The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules.
P2860
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P2860
Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters.
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Understanding the rates of cer ...... reactions of phosphodiesters.
@ast
Understanding the rates of cer ...... reactions of phosphodiesters.
@en
Understanding the rates of cer ...... reactions of phosphodiesters.
@nl
type
label
Understanding the rates of cer ...... reactions of phosphodiesters.
@ast
Understanding the rates of cer ...... reactions of phosphodiesters.
@en
Understanding the rates of cer ...... reactions of phosphodiesters.
@nl
prefLabel
Understanding the rates of cer ...... reactions of phosphodiesters.
@ast
Understanding the rates of cer ...... reactions of phosphodiesters.
@en
Understanding the rates of cer ...... reactions of phosphodiesters.
@nl
P356
P1433
P1476
Understanding the rates of cer ...... reactions of phosphodiesters.
@en
P2093
P304
11943-11952
P356
10.1021/BI00096A001
P407
P577
1993-11-01T00:00:00Z