Details
| Stereochemistry | ABSOLUTE |
| Molecular Formula | C15H16O3 |
| Molecular Weight | 244.2857 |
| Optical Activity | UNSPECIFIED |
| Defined Stereocenters | 1 / 1 |
| E/Z Centers | 0 |
| Charge | 0 |
SHOW SMILES / InChI
SMILES
COC(=O)[C@@H](C)C1=CC=C2C=C(OC)C=CC2=C1
InChI
InChIKey=ZFYFBPCRUQZGJE-JTQLQIEISA-N
InChI=1S/C15H16O3/c1-10(15(16)18-3)11-4-5-13-9-14(17-2)7-6-12(13)8-11/h4-10H,1-3H3/t10-/m0/s1
| Molecular Formula | C15H16O3 |
| Molecular Weight | 244.2857 |
| Charge | 0 |
| Count |
|
| Stereochemistry | ABSOLUTE |
| Additional Stereochemistry | No |
| Defined Stereocenters | 1 / 1 |
| E/Z Centers | 0 |
| Optical Activity | UNSPECIFIED |
Naproxen methyl ester, a mixture of two isomers R and S, is the precursor of therapeutically important nonsteroidal anti-inflammatory drug naproxen. Naproxen methyl ester can be enantioselectively hydrolyzed by lipases or (S)-enantioselective esterase could catalyze the selective hydrolysis of the (S)-Naproxen methyl ester, giving optically pure (S)-naproxen. In addition, S-naproxen methyl ester is used as a tool for identification and determination of new stereo selective carboxylesterase activities.
Approval Year
Targets
| Primary Target | Pharmacology | Condition | Potency |
|---|---|---|---|
Target ID: esterase Sso-Est1 from S. solfataricus P1 Sources: https://www.ncbi.nlm.nih.gov/pubmed/19544040 |
Conditions
| Condition | Modality | Targets | Highest Phase | Product |
|---|---|---|---|---|
PubMed
| Title | Date | PubMed |
|---|---|---|
| Efficient production of (S)-naproxen with (R)-substrate recycling using an overexpressed carboxylesterase BsE-NP01. | 2010-11 |
|
| Carboxylic ester hydrolases from hyperthermophiles. | 2009-07 |
|
| Effects of alcohol and buffer treatments on the activity and enantioselectivity of Candida rugosa lipase. | 2009 |
|
| A parametric study on biphasic medium conditions for the enantioselective production of naproxen by Candida rugosa lipase. | 2007-04 |
|
| Use of stable emulsion to improve stability, activity, and enantioselectivity of lipase immobilized in a membrane reactor. | 2003-12-20 |
|
| Effect of immobilization site and membrane materials on multiphasic enantiocatalytic enzyme membrane reactors. | 2003-03 |
|
| Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate-enzyme interaction. | 2002-08 |
Patents
| Substance Class |
Chemical
Created
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admin
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Edited
Mon Mar 31 22:11:01 GMT 2025
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Mon Mar 31 22:11:01 GMT 2025
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| Record UNII |
571OJX4PDN
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| Record Status |
Validated (UNII)
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9899603
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DTXSID50180780
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26159-35-3
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PARENT -> IMPURITY |
UNSPECIFIED
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PARENT -> IMPURITY |