129894-63-9 Usage
General Description
Benzenemethanol, (S)-4-nitro-(aminomethyl) is a chemical compound with a molecular formula C8H9N3O3. It is a chiral compound, meaning it exists in two different forms that are mirror images of each other, with the (S)-form being the type discussed here. Benzenemethanol,-(aminomethyl)-4-nitro-,(S)- is used as a reagent in organic synthesis and is commonly used in the pharmaceutical industry for the production of various drugs. It is also known to exhibit antibacterial and antifungal properties, making it a potentially useful compound in the development of new medications. Additionally, it is used as a building block in the synthesis of various organic compounds.
Check Digit Verification of cas no
The CAS Registry Mumber 129894-63-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,9,8,9 and 4 respectively; the second part has 2 digits, 6 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 129894-63:
(8*1)+(7*2)+(6*9)+(5*8)+(4*9)+(3*4)+(2*6)+(1*3)=179
179 % 10 = 9
So 129894-63-9 is a valid CAS Registry Number.
129894-63-9Relevant articles and documents
Enantioselective Aminohydroxylation of Styrenyl Olefins Catalyzed by an Engineered Hemoprotein
Cho, Inha,Prier, Christopher K.,Jia, Zhi-Jun,Zhang, Ruijie K.,G?rbe, Tamás,Arnold, Frances H.
supporting information, p. 3138 - 3142 (2019/02/01)
Chiral 1,2-amino alcohols are widely represented in biologically active compounds from neurotransmitters to antivirals. While many synthetic methods have been developed for accessing amino alcohols, the direct aminohydroxylation of alkenes to unprotected, enantioenriched amino alcohols remains a challenge. Using directed evolution, we have engineered a hemoprotein biocatalyst based on a thermostable cytochrome c that directly transforms alkenes to amino alcohols with high enantioselectivity (up to 2500 TTN and 90 % ee) under anaerobic conditions with O-pivaloylhydroxylamine as an aminating reagent. The reaction is proposed to proceed via a reactive iron-nitrogen species generated in the enzyme active site, enabling tuning of the catalyst's activity and selectivity by protein engineering.
