A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
about
Directed evolution of protein enzymes using nonhomologous random recombinationAncient Evolution and Recent Evolution Converge for the Biodegradation of Cyanuric Acid and Related TriazinesStructure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partnerpH 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.Investigating and Engineering Enzymes by Genetic Selection.Quantitative evaluation of noncovalent chorismate mutase-inhibitor binding by ESI-MS.Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection.Identification of key proteins and pathways in cadmium tolerance of Lactobacillus plantarum strains by proteomic analysisToward accurate screening in computer-aided enzyme design.A petunia chorismate mutase specialized for the production of floral volatiles.Aminobenzoates as building blocks for natural product assembly lines.Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Integrated transcriptomic and proteomic analysis of the bile stress response in a centenarian-originated probiotic Bifidobacterium longum BBMN68Pericyclic reactions catalyzed by chorismate-utilizing enzymes.Deciphering enzymes. Genetic selection as a probe of structure and mechanism.Preliminary X-ray crystallographic analysis of the secreted chorismate mutase from Mycobacterium tuberculosis: a tricky crystallization problem solved.Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid.The empirical valence bond as an effective strategy for computer-aided enzyme design.Unravelling potential virulence factor candidates in Xanthomonas citri. subsp. citri by secretome analysis.A label-free differential proteomics analysis reveals the effect of melatonin on promoting fruit ripening and anthocyanin accumulation upon postharvest in tomato.Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis.Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complexIdentification and analysis of seven effector protein families with different adaptive and evolutionary histories in plant-associated members of the Xanthomonadaceae.Probing protein environment in an enzymatic process: All-electron quantum chemical analysis combined with ab initio quantum mechanical/molecular mechanical modeling of chorismate mutase.The catalytic power of enzymes: conformational selection or transition state stabilization?
P2860
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P2860
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
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2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@ast
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@en
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@nl
type
label
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@ast
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@en
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@nl
prefLabel
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@ast
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@en
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@nl
P2093
P2860
P356
P1476
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
@en
P2093
P2860
P304
P356
10.1074/JBC.M006351200
P407
P50
P577
2000-11-24T00:00:00Z