Topic
Substrate (chemistry)
About: Substrate (chemistry) is a research topic. Over the lifetime, 35902 publications have been published within this topic receiving 740722 citations. The topic is also known as: enzyme substrate.
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TL;DR: The first sets of crystal structures of human SIRT3, an apo-structure with no substrate, a structure with a peptide containing acetyl lysine of its natural substrate acetyl-CoA synthetase 2, and a reaction intermediate structure trapped by a thioacetyl peptide, provide insights into the conformational changes induced by the two substrates required for the reaction.
178 citations
01 Apr 1987
TL;DR: This work presents a rapid, sensitive enzymatic assay for chloramphenicol acetyltransferase (CAT) that does not require chromatography, HPLC, or autoradiography, and is far more efficient for the performance of many assays, both in terms of labor and expense.
Abstract: We present a rapid, sensitive enzymatic assay for chloramphenicol acetyltransferase (CAT) that does not require chromatography, HPLC, or autoradiography. The assay is based on the use of an inexpensive substrate, tritiated acetate, instead of [14C]chloramphenicol. The method is adapted from one originally used by de Crombrugghe et al. (1973) and by Shaw (1975), but with simplifications appropriate for routine use. In our hands, the method is as sensitive as the customary thin-layer chromatography assay and is far more efficient for the performance of many assays, both in terms of labor and expense.
178 citations
TL;DR: The purification and properties of α-glucosidase from Saccharomyces italicus Y1225 have been studied and it is suggested that substrate hydrolysis involves an ionizable group of pKa 6.6–6.8.
178 citations
Patent•
29 May 2009
TL;DR: In this article, the authors discuss methods of decontaminating a surface comprising such a material from a chemical substrate of an enzyme such as a lipid or an organophosphorus compound, as well as reducing the growth of a microorganism on or within the material.
Abstract: Disclosed herein are a materials such as a coating, an elastomer, an adhesive, a sealant, a textile finish, a wax, and a filler for such a material, wherein the material includes an enzyme such as an esterase (e.g., a lipolytic enzyme, a sulfuric ester hydrolase, an organophosphorus compound degradation enzyme), an enzyme that degrades a cell wall and/or a cell membrane component (e.g., a lysozyme, a lytic transgrycosylase, a peptidase), and/or a biocidal or biostatic peptide. Also disclosed herein are methods of decontaminating a surface comprising such a material from a chemical substrate of an enzyme such as a lipid or an organophosphorus compound, as well as reducing the growth of a microorganism on or within such a material.
178 citations
Abstract: A numerical model for the substrate generation/tip collection (SG/TC) mode of the scanning electrochemical microscope (SECM), with amperometric electrodes, is developed and examined experimentally. Under the conditions of interest, this mode involves the diffusion-limited electrolysis of a solution species, R, to produce O, at a macroscopic substrate (generator) electrode. As O diffuses away, a fraction of the species is intercepted by a tip (collector) ultramicroelectrode (UME), positioned above the substrate, where the reverse reaction occurs, leading to the formation and diffusional feedback of R to the substrate. The time-dependent tip current response is shown to be sensitive to the ratio of diffusion coefficients of the O/R couple. Moreover, when the long-time (steady-state) tip current, determined under these conditions, is combined with measurements of the diffusion-limited current for the electrolysis of R at a tip positioned far from the substrate, differences in the diffusion coefficients of th...
177 citations