150737-17-0

Basic information

• Product Name: rac 4-Hydroxy-9-cis-retinoic Acid
• Synonyms: rac 4-Hydroxy-9-cis-retinoic Acid
• CAS NO: 150737-17-0
• Molecular Formula: C₂₀H₂₈O₃
• Molecular Weight: 316.43452
• Product Categories: Intermediates & Fine Chemicals;Metabolites & Impurities;Pharmaceuticals;Retinoids;Metabolites & Impurities, Pharmaceuticals, Intermediates & Fine Chemicals, Retinoids
• Mol File: 150737-17-0.mol
• Article Data: 7

Chemical Properties

• Melting Point: 130-133°C
• Boiling Point: 506.5°C at 760 mmHg
• Flash Point: 274.2°C
• Appearance: /
• Density: 1.075g/cm³
• Vapor Pressure: 2.22E-12mmHg at 25°C
• Refractive Index: 1.574
• Storage Temp.: Amber Vial, -20?C Freezer, Under Inert Atmosphere
• Solubility: Chloroform (Slightly), Methanol (Slightly)
• CAS DataBase Reference: rac 4-Hydroxy-9-cis-retinoic Acid(CAS DataBase Reference)
• NIST Chemistry Reference: rac 4-Hydroxy-9-cis-retinoic Acid(150737-17-0)
• EPA Substance Registry System: rac 4-Hydroxy-9-cis-retinoic Acid(150737-17-0)

Safety Data

• Hazardous Substances Data: 150737-17-0(Hazardous Substances Data)

Usage

Chemical Properties

Yellow Solid

Uses

A metabolite of 9-cis-Retinoic acid (R245000).

InChI:InChI=1/C20H28O3/c1-14(7-6-8-15(2)13-19(22)23)9-10-17-16(3)18(21)11-12-20(17,4)5/h6-10,13,18,21H,11-12H2,1-5H3,(H,22,23)/b8-6+,10-9+,14-7-,15-13+

Upstream product

• 68-26-8 RETINOL 
• 116-31-4 all-trans-Retinal 
• 302-79-4 all-trans-retinoic-acid 
• 38030-57-8 4-ketoretinoic acid 
• 72526-76-2 ethyl (2E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethyl-3-oxo-1-cyclohexen-1-yl)-2,4,6,8-nonatetraenoate 
• 63184-93-0 (2E,4E)-<5-(2,6,6-trimethyl-3-oxo-1-cyclohexen-1-yl)-3-methyl-2,4-pentadien-1-yl>triphenylphosphonium bromide 
• 81121-19-9 (2E,4E,6E,8E)-9-(3-Acetoxy-2,6,6-trimethyl-cyclohex-1-enyl)-3,7-dimethyl-nona-2,4,6,8-tetraenoic acid ethyl ester 
• 81121-21-3 rac-(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethyl-3-hydroxy-1-cyclohexen-1-yl)-2,4,6,8-nonatetraenoic acid ethyl ester 

Downstream Products

• 1425830-36-9 C₂₀H₂₈O₃ 
• 1425830-47-2 C₂₀H₂₈O₃ 
• 81121-27-9 rac-(2E,4E,6E,8E)-3,7-dimethyl-9-<2,6-dimethyl-6-(hydroxymethyl)-3-oxo-1-cyclohexen-1-yl>-2,4,6,8-nonatetraenoic acid 
• 38030-57-8 4-ketoretinoic acid 
• 38030-59-0 4-Hydroxyretinoic acid methyl ester 

Relevant articles and documents

CYP26C1 is a hydroxylase of multiple active retinoids and interacts with cellular retinoic acid binding proteins

The clearance of retinoic acid (RA) and its metabolites is believed to be regulated by the CYP26 enzymes, but the specific roles of CYP26A1, CYP26B1, and CYP26C1 in clearing active vitamin A metabolites have not been defined. The goal of this study was to

Stereoselective formation and metabolism of 4-hydroxy-retinoic acid enantiomers by cytochrome p450 enzymes

All-trans-retinoic acid (atRA), the major active metabolite of vitamin A, plays a role in many biological processes, including maintenance of epithelia, immunity, and fertility and regulation of apoptosis and cell differentiation. atRA is metabolized mainly by CYP26A1, but other P450 enzymes such as CYP2C8 and CYP3As also contribute to atRA 4-hydroxylation. Although the primary metabolite of atRA, 4-OH-RA, possesses a chiral center, the stereochemical course of atRA 4-hydroxylation has not been studied previously. (4S)- and (4R)-OH-RA enantiomers were synthesized and separated by chiral column HPLC. CYP26A1 was found to form predominantly (4S)-OH-RA. This stereoselectivity was rationalized via docking of atRA in the active site of a CYP26A1 homology model. The docked structure showed a well defined niche for atRA within the active site and a specific orientation of the β-ionone ring above the plane of the heme consistent with stereoselective abstraction of the hydrogen atom from the pro-(S)-position. In contrast to CYP26A1, CYP3A4 formed the 4-OH-RA enantiomers in a 1:1 ratio and CYP3A5 preferentially formed (4R)-OH-RA. Interestingly, CYP3A7 and CYP2C8 preferentially formed (4S)-OH-RA from atRA. Both (4S)- and (4R)-OH-RA were substrates of CYP26A1 but (4S)-OH-RA was cleared 3-fold faster than (4R)-OH-RA. In addition, 4-oxo-RA was formed from (4R)-OH-RA but not from (4S)-OH-RA by CYP26A1. Overall, these findings show that (4S)-OH-RA is preferred(4R)-OH-RA by the enzymes regulating atRA homeostasis. The stereoselectivity observed in CYP26A1 function will aid in better understanding of the active site features of the enzyme and the disposition of biologically active retinoids.

All-Trans-Retinol: All-Trans-13,14-Dihydroretinol Saturase and Methods of Its Use

Compositions of all-trans-retinol: all-trans-13,14-dihydroretinal saturase and methods of use thereof are provided.