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22038-87-5

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22038-87-5 Usage

Uses

Different sources of media describe the Uses of 22038-87-5 differently. You can refer to the following data:
1. (R)-1-(4-NITRO-PHENYL)-ETHYLAMINE is used in the synthesis of Tamsulosin (T006351).
2. R-(+)-α-Methyl-4-nitrobenzylamine is used in the synthesis of Tamsulosin (T006351).

Check Digit Verification of cas no

The CAS Registry Mumber 22038-87-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,2,0,3 and 8 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 22038-87:
(7*2)+(6*2)+(5*0)+(4*3)+(3*8)+(2*8)+(1*7)=85
85 % 10 = 5
So 22038-87-5 is a valid CAS Registry Number.
InChI:InChI=1/C8H10N2O2/c1-6(9)7-2-4-8(5-3-7)10(11)12/h2-6H,9H2,1H3/t6-/m1/s1

22038-87-5SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name R-(+)-α-Methyl-4-nitrobenzylamine

1.2 Other means of identification

Product number -
Other names (1R)-1-(4-nitrophenyl)ethanamine

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:22038-87-5 SDS

22038-87-5Relevant articles and documents

Widely applicable background depletion step enables transaminase evolution through solid-phase screening

Planchestainer, Matteo,Hegarty, Eimear,Heckmann, Christian M.,Gourlay, Louise J.,Paradisi, Francesca

, p. 5952 - 5958 (2019/06/19)

Directed evolution of transaminases is a widespread technique in the development of highly sought-after biocatalysts for industrial applications. This process, however, is challenged by the limited availability of effective high-throughput protocols to evaluate mutant libraries. Here we report a rapid, reliable, and widely applicable background depletion method for solid-phase screening of transaminase variants, which was successfully applied to a transaminase from Halomonas elongata (HEWT), evolved through rounds of random mutagenesis towards a series of diverse prochiral ketones. This approach enabled the identification of transaminase variants in viable cells with significantly improved activity towards para-substituted acetophenones (up to 60-fold), as well as tetrahydrothiophen-3-one and related substrates. Rationalisation of the mutants was assisted by determination of the high-resolution wild-type HEWT crystal structure presented herein.

Enantioselective synthesis of amines via reductive amination with a dehydrogenase mutant from Exigobacterium sibiricum: Substrate scope, co-solvent tolerance and biocatalyst immobilization

L?we, Jana,Ingram, Aaron A.,Gr?ger, Harald

, p. 1387 - 1392 (2018/03/21)

In recent years, the reductive amination of ketones in the presence of amine dehydrogenases emerged as an attractive synthetic strategy for the enantioselective preparation of amines starting from ketones, an ammonia source, a reducing reagent and a cofactor, which is recycled in situ by means of a second enzyme. Current challenges in this field consists of providing a broad synthetic platform as well as process development including enzyme immobilization. In this contribution these issues are addressed. Utilizing the amine dehydrogenase EsLeuDH-DM as a mutant of the leucine dehydrogenase from Exigobacterium sibiricum, a range of aryl-substituted ketones were tested as substrates revealing a broad substrate tolerance. Kinetics as well as inhibition effects were also studied and the suitability of this method for synthetic purpose was demonstrated with acetophenone as a model substrate. Even at an elevated substrate concentration of 50 mM, excellent conversion was achieved. In addition, the impact of water-miscible co-solvents was examined, and good activities were found when using DMSO of up to 30% (v/v). Furthermore, a successful immobilization of the EsLeuDH-DM was demonstrated utilizing a hydrophobic support and a support for covalent binding, respectively, as a carrier.

Biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases

Galman, James L.,Slabu, Iustina,Weise, Nicholas J.,Iglesias, Cesar,Parmeggiani, Fabio,Lloyd, Richard C.,Turner, Nicholas J.

supporting information, p. 361 - 366 (2017/08/14)

The discovery and characterisation of enzymes with both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals.

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