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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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Journal ArticleDOI
TL;DR: In this article, a review of the processes occurring on the treatment of triphenylphosphane with tetrachloromethane are first reported; a key role is played here by (trichlormethyl)phosphonium chloride which reacts with a further amount of the phosphane to give the stable salt [chloro(triphenyl phos-phoranediyl)methyl]triphenynphosphoni chloride by way of dichlorophosphorane and (dichloromethemylene)ph phosphorane that is detectable only
Abstract: In this review the processes occurring on the treatment of triphenylphosphane with tetrachloromethane are first reported; a key role is played here by (trichloromethyl)phosphonium chloride which reacts with a further amount of the phosphane to give the stable salt [chloro(triphenylphos-phoranediyl)methyl]triphenylphosphonium chloride by way of dichlorophosphorane and (dichloromethylene)phosphorane that is detectable only as an intermediate. The preparative application of the two-component system as a chlorinating, dehydrating, and P—N-linking reagent is ascribable to “phosphorylation” of the substrate in question through several reactive species. In these applications the reactions with the substrate compete with reactions of the two-component system with itself, so that the overall course of the reaction is in nearly all cases much more complex than was previously assumed. Nevertheless. very good results can be achieved by the use of this reagent, high yields and mild reaction conditions being characteristic.

784 citations

Journal ArticleDOI
TL;DR: A general rate equation has been derived and shown to be quadratic with square and linear terms in v which represents that true initial steady-state velocity of enzymic reactions that are reversibly inhibited by a substrate analogue at concentrations comparable to that of the enzyme.

773 citations

Journal ArticleDOI
TL;DR: Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB ofThe oxygenated enzyme.
Abstract: Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in complex with the inhibitor phenylthiourea were analyzed. The catalytic copper center is accommodated in a central four-helix-bundle located in a hydrophobic pocket close to the surface. Both metal binding sites are composed of three histidine ligands. His 109, ligated to the CuA site, is covalently linked to Cys 92 by an unusual thioether bond. Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB of the oxygenated enzyme.

749 citations

Journal ArticleDOI
TL;DR: In assays of the human matrix metalloproteinases, Mca‐Pro‐ Leu‐Gly‐Leu‐Dpa‐Ala‐Arg‐NH2 is about 50 to 100 times more sensitive than dinitrophenyl‐Pro •Leu •Gly •LeU‐Trp •Ala •d‐Arg •NH2 and continuous assays can be made at enzyme concentrations comparable to those used with macromolecular substrates.

739 citations

Journal ArticleDOI
TL;DR: A Mn(II)-dependent peroxidase found in the extracellular medium of ligninolytic cultures of the white rot fungus, Phanerochaete chrysosporium, was purified and the absorption spectrum of the enzyme indicates the presence of a heme prosthetic group.

716 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202214
2021807
20201,053
20191,064
20181,112
20171,024