127911-30-2

Basic information

• Product Name: (9R,10E,12Z)-9-hydroxy-10,12-octadecadienoic acid
• CAS NO: 127911-30-2
• Molecular Weight: 296.45
• Mol File: 127911-30-2.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: (9R,10E,12Z)-9-hydroxy-10,12-octadecadienoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (9R,10E,12Z)-9-hydroxy-10,12-octadecadienoic acid(127911-30-2)
• EPA Substance Registry System: (9R,10E,12Z)-9-hydroxy-10,12-octadecadienoic acid(127911-30-2)

Safety Data

• Hazardous Substances Data: 127911-30-2(Hazardous Substances Data)

Upstream product

• 2420-55-5 linoleic acid 
• 60-33-3 linoleic acid 
• 628-71-7 1-Heptyne 
• 137284-16-3 (E)-9-Acetoxy-11-bromo-undec-10-enoic acid butyl ester 
• 870-09-7 Heleninolsaeure-methylester 
• 137284-31-2 (E)-(R)-11-Bromo-9-hydroxy-undec-10-enoic acid 
• 6084-82-8 (R)-9-hydroxy-(10E,12Z)-10,12-octadecadienoic acid methyl ester 

Relevant articles and documents

Lipase Catalysed Regio- and Enantio-selective Hydrolysis: Molecular Recognition Phenomenon and Synthesis of (R)-Dimorphecolic Acid

Molecular recognition has been observed in hydrolysis of racemic esters of (E)-9=acetoxy-11-bromoundec-10-enoic acid by a lipase of Candida cylindracea (E.C. 3.1.1.3) where optically active (R)-(E)-9-acetoxy-11-bromoundec-10-enoic acid 99percent> was obtained which was used in synthesis of (R)-dimorphecolic acid.

Identification of an amino acid determinant of pH regiospecificity in a seed lipoxygenase from Momordica charantia

Lipoxygenases (LOX) form a heterogeneous family of lipid peroxidizing enzymes, which catalyze specific dioxygenation of polyunsaturated fatty acids. According to their positional specificity of linoleic acid oxygenation plant LOX have been classified into linoleate 9- and linoleate 13-LOX and recent reports identified a critical valine at the active site of 9-LOX. In contrast, more bulky phenylalanine or histidine residues were found at this position in 13-LOX. We have recently cloned a LOX-isoform from Momordica charantia and multiple amino acid alignments indicated the existence of a glutamine (Gln599) at the position were 13-LOX usually carry histidine or phenylalanine residues. Analyzing the pH-dependence of the positional specificity of linoleic acid oxygenation we observed that at pH-values higher than 7.5 this enzyme constitutes a linoleate 13-LOX whereas at lower pH, 9-H(P)ODE was the major reaction product. Site-directed mutagenesis of glutamine 599 to histidine (Gln599His) converted the enzyme to a pure 13-LOX. These data confirm previous observation suggesting that reaction specificity of certain LOX-isoforms is not an absolute enzyme property but may be impacted by reaction conditions such as pH of the reaction mixture. We extended this concept by identifying glutamine 599 as sequence determinant for such pH-dependence of the reaction specificity. Although the biological relevance for this alteration switch remains to be investigated it is of particular interest that it occurs at near physiological conditions in the pH-range between 7 and 8.