Pub. Date : 2017
PMID : 28085964
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The kinetic parametors kcat, Vmax and kcat/Km in the OPH reaction were remarkably increased in the buffers (pH 8.0, 25 C) containing aminoalcohols with C2 between nitrogen (N) and oxygen (O) in their structures, including triethanolamine (TEA), diethanolamine, monoethanolamine, 1-amino-2-propanol, 2-amino-2-methyl-1-propanol, and triisopropanolamine. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 2 | The kinetic parametors kcat, Vmax and kcat/Km in the OPH reaction were remarkably increased in the buffers (pH 8.0, 25 C) containing aminoalcohols with C2 between nitrogen (N) and oxygen (O) in their structures, including triethanolamine (TEA), diethanolamine, monoethanolamine, 1-amino-2-propanol, 2-amino-2-methyl-1-propanol, and triisopropanolamine. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 3 | The 300 mM TEA further increased DFP-degrading activities of OPH mutants F132Y and L140Y, the previously reported OPH mutants with desirable activities towards DFP. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 4 | The 300 mM TEA further increased DFP-degrading activities of OPH mutants F132Y and L140Y, the previously reported OPH mutants with desirable activities towards DFP. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 5 | However, the treatment of ethylenediaminetetraacetate (EDTA) markedly abolished the TEA-induced activation of OPH. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |
| 6 | The product fluoride effectively inhibited OPH-catalyzed hydrolysis of DFP by a linear mixed inhibition (inhibition constant Ki ~ 3.21 mM), which was partially released by TEA adding at initial or later reaction stage. | triethanolamine | acylaminoacyl-peptide hydrolase | Homo sapiens |