77977-73-2 Usage
General Description
(R)-4-Nitromandelic acid is a chemical compound with the molecular formula C8H7NO5. It is a chiral compound, meaning it has a non-superimposable mirror image. (R)-4-NITROMANDELIC ACID is derived from mandelic acid and contains a nitro group, which gives it unique properties and potential applications. It is used in the synthesis of various pharmaceuticals and organic compounds and has been studied for its potential biological activities. Additionally, it can also act as a ligand in metal complexation reactions and is important in the field of coordination chemistry. Overall, (R)-4-Nitromandelic acid is a versatile compound with various applications in different areas of chemistry and pharmaceuticals.
Check Digit Verification of cas no
The CAS Registry Mumber 77977-73-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,7,9,7 and 7 respectively; the second part has 2 digits, 7 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 77977-73:
(7*7)+(6*7)+(5*9)+(4*7)+(3*7)+(2*7)+(1*3)=202
202 % 10 = 2
So 77977-73-2 is a valid CAS Registry Number.
InChI:InChI=1/C8H7NO5/c10-7(8(11)12)5-1-3-6(4-2-5)9(13)14/h1-4,7,10H,(H,11,12)/t7-/m0/s1
77977-73-2Relevant articles and documents
Oxalyl-CoA Decarboxylase Enables Nucleophilic One-Carbon Extension of Aldehydes to Chiral α-Hydroxy Acids
Burgener, Simon,Cortina, Ni?a Socorro,Erb, Tobias J.
supporting information, p. 5526 - 5530 (2020/02/20)
The synthesis of complex molecules from simple, renewable carbon units is the goal of a sustainable economy. Here we explored the biocatalytic potential of the thiamine-diphosphate-dependent (ThDP) oxalyl-CoA decarboxylase (OXC)/2-hydroxyacyl-CoA lyase (HACL) superfamily that naturally catalyzes the shortening of acyl-CoA thioester substrates through the release of the C1-unit formyl-CoA. We show that the OXC/HACL superfamily contains promiscuous members that can be reversed to perform nucleophilic C1-extensions of various aldehydes to yield the corresponding 2-hydroxyacyl-CoA thioesters. We improved the catalytic properties of Methylorubrum extorquens OXC by rational enzyme engineering and combined it with two newly described enzymes—a specific oxalyl-CoA synthetase and a 2-hydroxyacyl-CoA thioesterase. This enzymatic cascade enabled continuous conversion of oxalate and aromatic aldehydes into valuable (S)-α-hydroxy acids with enantiomeric excess up to 99 %.
