p-chloromercuribenzoic acid has been researched along with serine in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 1 (20.00) | 2.80 |
Authors | Studies |
---|---|
Drijfhout, MC; Eppink, MH; Hagen, WR; van Berkel, WJ; van der Bolt, FJ | 1 |
Ishii, Y; Miura, T; Mori, T; Noguchi, Y; Saito, Y; Yamada, H | 1 |
Kleineidam, RG; Kruse, S; Pommerencke, J; Roggentin, P; Schauer, R | 1 |
Masuda, T; Ohta, H; Shimada, H; Suzuki, T; Takamiya, K; Tsuchiya, T; Yamada, T | 1 |
Badepally, NG; Singh, A; Surolia, A | 1 |
5 other study(ies) available for p-chloromercuribenzoic acid and serine
Article | Year |
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Selective cysteine-->serine replacements in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens allow the unambiguous assignment of Cys211 as the site of modification by spin-labeled p-chloromercuribenzoate.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Base Sequence; Catalysis; Chloromercuribenzoates; Cysteine; Electron Spin Resonance Spectroscopy; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; p-Chloromercuribenzoic Acid; Pseudomonas fluorescens; Serine; Spin Labels; Structure-Activity Relationship | 1994 |
Protein engineering of a cephalosporin C acylase.
Topics: Amidohydrolases; Bioreactors; Chloromercuribenzoates; Cysteine; Enzyme Inhibitors; Enzymes, Immobilized; Kinetics; Mutagenesis, Site-Directed; p-Chloromercuribenzoic Acid; Penicillin Amidase; Protein Engineering; Pseudomonas; Serine; Structure-Activity Relationship; Sulfhydryl Reagents | 1996 |
Effect of cysteine modifications on the activity of the 'small' Clostridium perfringens sialidase.
Topics: Amino Acid Sequence; Clostridium perfringens; Cysteine; Ethylmaleimide; Gram-Positive Bacteria; Kinetics; Mercuric Chloride; Molecular Sequence Data; Mutagenesis, Site-Directed; Neuraminidase; p-Chloromercuribenzoic Acid; Recombinant Proteins; Sequence Homology, Amino Acid; Serine; Structure-Activity Relationship; Substrate Specificity | 1998 |
Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad.
Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Carboxylic Ester Hydrolases; Catalysis; Chenopodium album; Enzyme Inhibitors; Histidine; Hydrolysis; Isoflurophate; Lipase; Molecular Sequence Data; Morpholines; Mutagenesis, Site-Directed; Mutation; p-Chloromercuribenzoic Acid; Phenylmethylsulfonyl Fluoride; Sequence Homology, Amino Acid; Serine; Serine Endopeptidases | 2003 |
Role of a cysteine residue in substrate entry and catalysis in MtHIBADH: Analysis by chemical modifications and site-directed mutagenesis.
Topics: Alanine; Alcohol Oxidoreductases; Bacterial Proteins; Catalysis; Cysteine; Dinitrobenzenes; Hydrogen Bonding; Models, Molecular; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; NAD; p-Chloromercuribenzoic Acid; Protein Conformation; Recombinant Proteins; Serine; Structure-Activity Relationship; Substrate Specificity | 2021 |