32459-66-8

Basic information

• Product Name: 11-HYDROXY LAURIC ACID
• Synonyms: 11-HYDROXY LAURIC ACID;11-hydroxydodecanoic acid;(ω-1)-Hydroxylauric acid;KQGAHNAFXMVSGY-UHFFFAOYSA-N
• CAS NO: 32459-66-8
• Molecular Formula: C₁₂H₂₄O₃
• Molecular Weight: 216.32
• Product Categories: Aliphatics, Pharmaceuticals, Intermediates & Fine Chemicals
• Mol File: 32459-66-8.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 353.2°Cat760mmHg
• Flash Point: 181.6°C
• Appearance: /
• Density: 0.987g/cm³
• Vapor Pressure: 2.12E-06mmHg at 25°C
• Refractive Index: 1.466
• Storage Temp.: -20°C Freezer, Under inert atmosphere
• Solubility: DMSO (Slightly), Ethyl Acetate (Slightly), Methanol (Slightly)
• CAS DataBase Reference: 11-HYDROXY LAURIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 11-HYDROXY LAURIC ACID(32459-66-8)
• EPA Substance Registry System: 11-HYDROXY LAURIC ACID(32459-66-8)

Safety Data

• Hazardous Substances Data: 32459-66-8(Hazardous Substances Data)

Usage

Description

11-Hydroxy Lauric Acid is a medium-chain fatty acid that is lauric acid substituted at position 11 by a hydroxy group. It is a naturally occurring compound with unique chemical properties and potential applications in various fields.

Uses

Used in Pharmaceutical Industry:
11-Hydroxy Lauric Acid is used as a substrate for the functional expression and characterization of cytochrome P450 52A21, an enzyme involved in the metabolism of various drugs and compounds. This application is crucial for understanding the enzyme's role in drug metabolism and its potential implications in drug efficacy and safety.
Used in Research and Development:
11-Hydroxy Lauric Acid serves as a valuable compound for research purposes, particularly in the study of fatty acid metabolism, enzyme function, and the development of new drugs and therapies. Its unique structure and properties make it an interesting subject for scientific investigation and potential applications in medicine and biotechnology.

InChI:InChI=1/C12H24O3/c1-11(13)9-7-5-3-2-4-6-8-10-12(14)15/h11,13H,2-10H2,1H3,(H,14,15)

Upstream product

• 143-07-7 lauric acid 
• 629-25-4 Sodium laurate 

Relevant articles and documents

Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119

CYP119, a cytochrome P450 from a thermophilic organism for which a crystal structure is available, is shown here to hydroxylate lauric acid in a reaction supported by putidaredoxin and putidaredoxin reductase. This fatty acid hydroxylation activity is increased 15-fold by T214V and D77R mutations. The T214V mutation increases the rate by facilitating substrate binding and enhancing the associated spin state change, whereas the D77R mutation improves binding of the heterologous redox partner putidaredoxin to CYP119 and the rate of electron transfer from it to the heme group. A sequence alignment with P450cam can, therefore, be used to identify a part of the binding site for putidaredoxin on an unrelated P450 enzyme. This information can be used to engineer by mutagenesis an improved complementarity of the protein-protein interface that results in improved electron transfer from putidaredoxin to the P450 enzyme. As a result, the catalytic activity of the thermo- and barostable CYP119 has been incorporated into a catalytic system that hydroxylates fatty acids.

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: Implications for the mechanism of electron transfer in the P450 BM3 dimer

Bacillus megaterium P450 BM3 (BM3) is a P450/P450 reductase fusion enzyme, where the dimer is considered the active form in NADPH-dependent fatty acid hydroxylation. The BM3 W1046A mutant was generated, removing an aromatic "shield" from its FAD isoalloxazine ring. W1046A BM3 is a catalytically active NADH-dependent lauric acid hydroxylase, with product formation slightly superior to the NADPH-driven enzyme. The W1046A BM3 K m for NADH is 20-fold lower than wild-type BM3, and catalytic efficiency of W1046A BM3 with NADH and NADPH are similar in lauric acid oxidation. Wild-type BM3 also catalyzes NADH-dependent lauric acid hydroxylation, but less efficiently than W1046A BM3. A hypothesis that W1046A BM3 is inactive [15] helped underpin a model of electron transfer from FAD in one BM3 monomer to FMN in the other in order to drive fatty acid hydroxylation in native BM3. Our data showing W1046A BM3 is a functional fatty acid hydroxylase are consistent instead with a BM3 catalytic model involving electron transfer within a reductase monomer, and from FMN of one monomer to heme of the other [12]. W1046A BM3 is an efficient NADH-utilizing fatty acid hydroxylase with potential biotechnological applications.

Regio- and Enantio-selective Chemo-enzymatic C?H-Lactonization of Decanoic Acid to (S)-δ-Decalactone

The conversion of saturated fatty acids to high value chiral hydroxy-acids and lactones poses a number of synthetic challenges: the activation of unreactive C?H bonds and the need for regio- and stereoselectivity. Here the first example of a wild-type cytochrome P450 monooxygenase (CYP116B46 from Tepidiphilus thermophilus) capable of enantio- and regioselective C5 hydroxylation of decanoic acid 1 to (S)-5-hydroxydecanoic acid 2 is reported. Subsequent lactonization yields (S)-δ-decalactone 3, a high value fragrance compound, with greater than 90 % ee. Docking studies provide a rationale for the high regio- and enantioselectivity of the reaction.