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方案
95%
反应适用性
reaction type: Coupling Reactions
mp
220 °C (dec.) (lit.)
应用
peptide synthesis
SMILES字符串
CC[n+]1ccc(o1)-c2cccc(c2)S([O-])(=O)=O
InChI
1S/C11H11NO4S/c1-2-12-7-6-11(16-12)9-4-3-5-10(8-9)17(13,14)15/h3-8H,2H2,1H3
InChI key
MWOOKDULMBMMPN-UHFFFAOYSA-N
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
S R Rao et al.
Indian journal of biochemistry & biophysics, 34(3), 253-258 (1997-06-01)
Maize leaf NADP-malic enzyme was rapidly inactivated by micromolar concentrations of Woodward's reagent K (WRK). The inactivation followed pseudo-first order reaction kinetics. The order of reaction with respect to WRK was 1, suggesting that inactivation was a consequence of the
Paulina Nawłoka et al.
Acta biochimica Polonica, 50(2), 567-572 (2003-07-02)
Effects of several chemical probes selectively modifying various amino-acid residues on the activity of UDP-glucose : solasodine glucosyltransferase from eggplant leaves was studied. It was shown that diethylpyrocarbonate (DEPC), a specific modifier of histidine residues, was strongly inhibitory. However, in
G Feller et al.
The Journal of biological chemistry, 271(39), 23836-23841 (1996-09-27)
Chloride is the allosteric effector of vertebrate pancreatic and salivary alpha-amylases and of the bacterial alpha-amylase from Alteromonas haloplanctis. Activation experiments of A. haloplanctis alpha-amylase by several monovalent anions show that a negative charge, not restricted to that of Cl-
Jongchan Woo et al.
Protein science : a publication of the Protein Society, 17(4), 725-735 (2008-03-25)
Renilla luciferase (RLUC) is a versatile tool for gene expression assays and in vivo biosensor applications, but its catalytic mechanism remains to be elucidated. RLUC is evolutionarily related to the alpha/beta hydrolase family. Its closest known homologs are bacterial dehalogenases
Hassan Faridnouri et al.
Bioelectrochemistry (Amsterdam, Netherlands), 82(1), 1-9 (2011-07-01)
This work describes the reaction mechanism for chemical modification of tyrosinase by Woodward's Reagent K and its covalent attachment to a glassy carbon electrode. The spectrophotometric studies revealed that the modification does not cause a significant structural change to tyrosinase.
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