49601-06-1 Usage
Uses
Used in Pharmaceutical Industry:
(S)-2-hydroxy-2-(isopropyl)succinic acid is used as a pharmaceutical intermediate for the synthesis of various drugs and biologically active compounds. Its chiral nature and hydroxy acid functionality contribute to the development of new medications with improved efficacy and selectivity.
Used in Chiral Building Blocks:
In the field of organic chemistry, (S)-2-hydroxy-2-(isopropyl)succinic acid is used as a chiral building block for the preparation of various chiral molecules. Its unique stereochemistry allows for the creation of complex molecular structures with specific biological activities.
Used in Asymmetric Synthesis:
(S)-2-hydroxy-2-(isopropyl)succinic acid is employed in asymmetric synthesis, a technique that allows for the selective production of one enantiomer over another. This is particularly important in the pharmaceutical industry, as the different enantiomers of a drug can have vastly different biological activities and side effects.
Used in Materials Science:
(S)-2-hydroxy-2-(isopropyl)succinic acid has been explored for its potential use in the development of new materials such as chiral liquid crystals. These materials have applications in various industries, including electronics, where they can be used in display technologies and sensors.
Check Digit Verification of cas no
The CAS Registry Mumber 49601-06-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,9,6,0 and 1 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 49601-06:
(7*4)+(6*9)+(5*6)+(4*0)+(3*1)+(2*0)+(1*6)=121
121 % 10 = 1
So 49601-06-1 is a valid CAS Registry Number.
InChI:InChI=1/C7H12O5/c1-4(2)7(12,6(10)11)3-5(8)9/h4,12H,3H2,1-2H3,(H,8,9)(H,10,11)/t7-/m0/s1
49601-06-1Relevant academic research and scientific papers
Huisman, Frances H.A.,Hunter, Michael F.C.,Devenish, Sean R.A.,Gerrard, Juliet A.,Parker, Emily J.
, p. 168 - 173 (2010)
α-Isopropylmalate synthase (α-IPMS) catalyses the first committed step in leucine biosynthesis in many pathogenic bacteria, including Neisseria meningitidis. This enzyme (NmeIPMS) has been purified, characterised, and compared to α-IPMS proteins from other bacteria. NmeIPMS is a homodimer which catalyses the condensation of α-ketoisovalerate (α-KIV) and acetyl coenzyme A (AcCoA), and is inhibited by leucine. NmeIPMS can use alternate α-ketoacids as substrates and, in contrast to α-IPMS from other sources, is activated by a range of metal ions including Cd2+ and Zn2+ that have previously been reported as inhibitory, since they suppress the dithiodipyridone assay system rather than the enzyme itself. Previous studies indicate that α-IPMS is a TIM barrel enzyme with an allosteric leucine-binding domain. To assess the importance of this domain, a truncated form of NmeIPMS was generated and characterised. Loss of the regulatory domain resulted in a loss of the ability to catalyse the aldol reaction, although the enzyme was still able to slowly hydrolyse AcCoA independently of α-KIV at a rate similar to that of the WT enzyme. This implies that the regulatory domain is not only required for control of enzymatic activity but may assist in the positioning of key residues in the catalytic TIM barrel. The importance of this domain to catalytic function may offer new strategies for inhibitor design.
