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76763-88-7

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76763-88-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 76763-88-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,6,7,6 and 3 respectively; the second part has 2 digits, 8 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 76763-88:
(7*7)+(6*6)+(5*7)+(4*6)+(3*3)+(2*8)+(1*8)=177
177 % 10 = 7
So 76763-88-7 is a valid CAS Registry Number.

76763-88-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name (R)-dihydro-4-(3,4,5-trimethoxybenzyl)furan-2(3H)-one

1.2 Other means of identification

Product number -
Other names (R)-3-[1-(3,4,5-trimethoxyphenyl)methyl]butanolide

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:76763-88-7 SDS

76763-88-7Relevant articles and documents

Type II flavin-containing monooxygenases: A new class of biocatalysts that harbors baeyer-villiger monooxygenases with a relaxed coenzyme specificity

Riebel, Anette,Fink, Michael J.,Mihovilovic, Marko D.,Fraaije, Marco W.

, p. 1112 - 1117 (2014/05/06)

Within a newly identified set of flavin-containing monooxygenases (FMOs) from Rhodococcus jostii RHA1, we have identified three monooxygenases (FMO-E, FMO-F, and FMO-G) that are effective in catalyzing Baeyer-Villiger oxidations. These type II FMOs display relaxed coenzyme specificity by accepting both NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) and NADH (reduced form of nicotinamide adenine dinucleotide), as a coenzyme, which is a novel and attractive feature among biocatalysts capable of conducting Baeyer-Villiger oxidations. We purified FMO-E and determined that the Michaelis constants for both coenzymes were in the micromolar range, whereas the activity was highest for NADH. By using the stopped-flow technique, formation of a peroxyflavin-enzyme intermediate was observed, which indicated that type II FMOs follow a catalytic mechanism similar to that of other class B flavoprotein monooxygenases. A set of cyclobutanones and cyclohexanones were used to probe the regio- and enantioselectivity of all three recombinant monooxygenases. The biocatalysts readily accepted small cyclic ketones, which enabled the conversion of previously poorly accepted substrates by other monooxygenases (especially norcamphor), and exhibited excellent and unique regio- and enantioselectivities. Sequence analysis revealed that type II FMOs that act as Baeyer-Villiger monooxygenases contain a unique N-terminal domain. Sequence conservation in this protein domain can be used to identify new NADH-dependent Baeyer-Villiger monooxygenases, which would facilitate future biocatalyst discovery efforts. New kid on the block: Members of a newly recognized group of sequence-related flavin-containing monooxygenases can perform Baeyer-Villiger oxidations. Their coenzyme indifference and unique specificity make them attractive biocatalysts.

Total Synthesis of Homochiral Kadsurin Having the Natural Configuration

Ohshima, Toshihiro,Tanaka, Masahide,Mitsuhashi, Hiroshi,Maruno, Masao,Wakamatsu, Takeshi

, p. 139 - 146 (2007/10/02)

The total synthesis of kadsurin was achieved in a stereoselective manner.The stereoselective hydrogenation of the homochiral enone (12), obtained from the known tetracyclic lactone (7), afforded known ketone (13), the conversion of which into kadsurin has

Asymmetric total synthesis of the antileukaemic lignan precursor (-)steganone and revision of its absolute configuration

Robin,Gringore,Brown

, p. 2709 - 2712 (2007/10/02)

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