Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines.
about
The chemical biology of protein phosphorylationUnusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidaseReaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reactionPromiscuous Partitioning of a Covalent Intermediate Common in the Pentein SuperfamilyComparative Analysis of Mutant Tyrosine Kinase Chemical Rescue † ‡Structure of alanine racemase fromOenococcus oeniwith bound pyridoxal 5′-phosphateChemical rescue and inhibition studies to determine the role of Arg301 in phosphite dehydrogenaseApplication of linear free energy relationships to the serpin-proteinase inhibition mechanismThe glmS ribozyme cofactor is a general acid-base catalystTrapping of peptide-based surrogates in an artificially created channel of cytochrome c peroxidase.The importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins.Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding.Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces.Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.Plasticity of acetylcholine receptor gating motions via rate-energy relationships.Light-enhanced catalysis by pyridoxal phosphate-dependent aspartate aminotransferase.Mutational and biochemical analysis of the DNA-entry nuclease EndA from Streptococcus pneumoniae.Chemical rescue, multiple ionizable groups, and general acid-base catalysis in the HDV genomic ribozyme.Mapping the limits of substrate specificity of the adenylation domain of TycA.Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysisBreaching the conformational integrity of the catalytic triad of the serine protease plasmin: localized disruption of a side chain of His-603 strongly inhibits the amidolytic activity of human plasmin.DNA-Catalyzed Amide HydrolysisEnzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferWhither Enzymology in the Twenty First Century?A chemo-genetic approach for the study of nucleobase participation in nucleolytic ribozymes.Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system.On the failure of de novo-designed peptides as biocatalysts.Rescue of abasic hammerhead ribozymes by exogenous addition of specific basesStructure-Reactivity Relationships for β-Galactosidase (Escherichia coli, lac Z): A Second Derivative Effect on β(nuc) for Addition of Alkyl Alcohols to an Oxocarbenium Ion Reaction Intermediate.The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.Aspartate aminotransferase: an old dog teaches new tricks.Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as established by chemical rescue experiments.Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase.Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II.Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a.Allosteric regulation of human liver pyruvate kinase by peptides that mimic the phosphorylated/dephosphorylated N-terminus.Mapping the conformational wave of acetylcholine receptor channel gating.Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127.BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".
P2860
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P2860
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@en
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@nl
type
label
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@en
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@nl
prefLabel
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@en
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@nl
P356
P1433
P1476
Direct Brønsted analysis of th ...... nt enzyme by exogenous amines.
@en
P2093
P304
P356
10.1126/SCIENCE.2538921
P407
P577
1989-03-01T00:00:00Z