Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine.
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Switching DNA-binding specificity by unnatural amino acid substitution.Structural Insights into the Recovery of Aldolase Activity inN-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis StrategyCrystal structure of the dopamine N -acetyltransferase–acetyl-CoA complex provides insights into the catalytic mechanismThe importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins.Maturation of IncP pilin precursors resembles the catalytic Dyad-like mechanism of leader peptidases.Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trappingModification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Regeneration of catalytic activity of glutamine synthetase mutants by chemical activation: exploration of the role of arginines 339 and 359 in activity.Chemical-modification rescue assessed by mass spectrometry demonstrates that gamma-thia-lysine yields the same activity as lysine in aldolase.Chloroplastic aspartate aminotransferase from Arabidopsis thaliana: an examination of the relationship between the structure of the gene and the spatial structure of the protein.Signal peptidase I: cleaving the way to mature proteins.Chemical mutagenesis of vaccinia DNA topoisomerase lysine 167 provides insights to the catalysis of DNA transesterification.Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies.Ribonuclease a: revealing structure-function relationships with semisynthesis.Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase.
P2860
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P2860
Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Reengineering the catalytic ly ...... netically introduced cysteine.
@en
Reengineering the catalytic ly ...... netically introduced cysteine.
@nl
type
label
Reengineering the catalytic ly ...... netically introduced cysteine.
@en
Reengineering the catalytic ly ...... netically introduced cysteine.
@nl
prefLabel
Reengineering the catalytic ly ...... netically introduced cysteine.
@en
Reengineering the catalytic ly ...... netically introduced cysteine.
@nl
P356
P1433
P1476
Reengineering the catalytic ly ...... netically introduced cysteine.
@en
P2093
P304
P356
10.1021/BI00247A023
P407
P577
1991-08-01T00:00:00Z