79-63-0 Usage
Description
Different sources of media describe the Description of 79-63-0 differently. You can refer to the following data:
1. Lanosterol occurs naturally in the eyes of mammals and has been shown to dissolve cataracts by revitalizing damaged cataract-causing crystallin proteins. Lanosterol’s amphipathic nature is believed to play a large role in its ability to prevent and reverse cataract formation.
2. Lanosterol is a naturally-occurring sterol and biosynthetic precursor of several animal, fungal, and protozoan steroids, including cholesterol and ergosterol. Defects in the processing of lanosterol contribute to a wide variety of disorders, including the formation of cataracts. Similarly, certain fungicides act by blocking lanosterol processing by fungi.
Source
Lanosterol is the first sterol in lipid biosynthetic pathway, which is initially converted by acetyl-CoA. The complex process of lanosterol synthesis involves several enzymes, including 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, squalene epoxidase, and lanosterol synthase (LSS). LSS is a microsomal enzyme that functions as a downstream element in the lanosterol biosynthetic pathway, catalyzing the cyclization of the linear 2,3-monoepoxysqualene to lanosterol.
Function
A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid (PubMed:20149798, PubMed:8619637). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase.
Biosynthesis pathway
The lanosterol pathway refers to a segment of the cholesterol biosynthesis pathway comprising twelve enzymes, namely acetyl-CoA acetyltransferase, hydroxymethylglutaryl-CoA synthase, hydroxymethylglutaryl-CoA reductase, mevalonate kinase, phosphomevalonate kinase, diphoshomevalonate decarboxylase, isopentenyl-diphosphate delta isomerase, geranylgeranyl diphosphate synthase, farnesyl diphosphate synthase, squalene synthase, squalene monooxygenase and lanosterol synthase. The lanosterol pathway describes the stages of cholesterol biosynthesis between the conversion of substrates acetyl CoA and acetoacetyl CoA to (S)-3-hydroxy-3-methylglutaryl-CoA, through to the formation of intermediate metabolite lanosterol, the precursor of cholesterol. Metabolites of the lanosterol pathway are either directed to the synthesis of cholesterol and other sterols, or to side branches of the pathway through which they are converted to isoprenoids and other non-sterols.
Uses
Lanosterol has been used:as a standard in HPLC for the quantification in testis samplesin S-adenosyl-L-methionine:Δ24-sterol-C-methyltransferase (SMT) assayto treat wild-type cells growing in rich medium to know its effects on Sre1 protein
Definition
ChEBI: A tetracyclic triterpenoid that is lanosta-8,24-diene substituted by a beta-hydroxy group at the 3beta position. It is the compound from which all steroids are derived.
General Description
Lanosterol, an amphipathic molecule, that is produced by?lanosterol?synthase (LSS). It is enriched in the lens.
Biochem/physiol Actions
Cholesterol precursor sterol.Lanosterol serves as an endogenous selective modulator of macrophage immunity.
Purification Methods
If very impure, then it should be acetylated, converted to the dibromide acetate [crystallised from EtOAc with slow cooling, m 168-170o, [] D +214o (CHCl3)], de-brominated with Zn dust to give the acetate (below) which is recrystallised from 3-4 parts of Me2CO/MeOH (4:1) and hydrolysed as for stigmasterol (below). Recrystallise it from anhydrous MeOH. Dry it in vacuo over P2O5 for 3hours at 90o. The purity is checked by proton magnetic resonance. The acetate crystallises from MeOH with m 131-133o and [ ] 25D +62o (c 1,CHCl3). [Block & Urech Biochemical Preparations 6 32 1958. van Tamelen et al. J Am Chem Soc 104 6479, 6480 1982, Beilstein 6 III 2880, 6 IV 4188.]
Check Digit Verification of cas no
The CAS Registry Mumber 79-63-0 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 7 and 9 respectively; the second part has 2 digits, 6 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 79-63:
(4*7)+(3*9)+(2*6)+(1*3)=70
70 % 10 = 0
So 79-63-0 is a valid CAS Registry Number.
InChI:InChI=1/C30H50O/c1-20(2)10-9-11-21(3)22-14-18-30(8)24-12-13-25-27(4,5)26(31)16-17-28(25,6)23(24)15-19-29(22,30)7/h10,21-22,25-26,31H,9,11-19H2,1-8H3/t21-,22?,25-,26-,28+,29-,30+/m0/s1
79-63-0Relevant articles and documents
Efficient cyclization of squalene epoxide to lanosterol with immobilized cells of baker's yeast
Rotthaus, Olaf,Demuth, Martin
, p. 7291 - 7293 (2002)
The cyclization of squalene epoxide to lanosterol with baker's yeast (Saccharomyces cerevisiae) can conveniently be carried out in aqueous solution with glass cored immobilisates of cells in calcium alginate. This enables the manifold use of the microorganism to obtain lanosterol in a single biocatalytic step using the immobilisates repeatedly.
Partial purification and characterization of oxidosqualene-lanosterol cyclase from baker's yeast
Hoshino,Williams,Chung,Scott
, p. 5925 - 5932 (1991)
Partial (120-fold) purification of oxidosqualene-lanosterol cyclase from yeast is described. The enzyme derived from the microsomal fraction converts 1 mM S-squalene oxide to lanosterol in 5 h and has a pH optimum of 6.2, lower than that (pH 7.2) of the hog-liver cyclase catalyzing the same reaction. Although the yeast cyclase is stimulated by high concentrations of potassium phosphate buffer, high concentrations of potassium or sodium chloride inhibit activity. The concentration range of Triton X-100 for optimal activity is 0.7-1.2%.
A well-defined monomeric aluminum complex as an efficient and general catalyst in the Meerwein-Ponndorf-Verley reduction
McNerney, Brian,Whittlesey, Bruce,Cordes, David B.,Krempner, Clemens
supporting information, p. 14959 - 14964 (2015/01/08)
The metal-catalyzed Meerwein-Ponndorf-Verley (MPV) reduction allows for the mild and sustainable reduction of aldehydes and ketones but has not found widespread application in organic synthesis due to the high catalyst loading often required to obtain satisfactory yields of the reduced product. We report here on the synthesis and structure of a sterically extremely overloaded siloxide-supported aluminum isopropoxide capable of catalytically reducing a wide range of aldehydes and ketones (52 examples) in excellent yields under mild conditions and with low catalyst loadings. The unseen activity of the developed catalyst system in MPV reductions is due to its unique monomeric nature and the neutral donor isopropanol weakly coordinating to the aluminum center. The present work implies that monomeric aluminum alkoxide catalysts may be attractive alternatives to transition-metalbased systems for the selective reduction of aldehydes and ketones to primary and secondary alcohols.
Sterol C24-methyltransferase: Physio- and stereo-chemical features of the sterol C3 group required for catalytic competence
Howard, Alicia L.,Liu, Jialin,Elmegeed, Gamal A.,Collins, Emily K.,Ganatra, Kalgi S.,Nwogwugwu, Chizaram A.,Nes, W. David
body text, p. 43 - 50 (2012/08/07)
Sterol C24-methyltransferases (24-SMTs) catalyze the electrophilic alkylation of Δ24-sterols to a variety of sterol side chain constructions, and the C3- moiety is the primary determinant for substrate binding by these enzymes. To determine what specific structural features of the C3-polar group ensure sterol catalysis, a series of structurally related C3-analogs of lanosterol that differed in stereochemistry, bulk and electronic properties were examined against the fungal 24-SMT from Paracoccidioides brasiliensis (Pb) which recognize lanosterol as the natural substrate. Analysis of the magnitude of sterol C24-methylation activity (based on the kinetic constants of Vmax/Km and product distributions determined by GC-MS) resulting from changes at the C3-position in which the 3β-OH was replaced by 3α-OH, 3β-acetyl, 3-oxo, 3-OMe, 3β-F, 3β-NH2 (protonated species) or 3H group revealed that lanosterol and five substrate analogs were catalyzed and yielded identical side chain products whereas neither the 3H- or 3α-OH lanosterol derivatives were productively bound. Taken together, our results demonstrate a chemical complementarity involving hydrogen bonding formation of specific active site contacts to the nucleophilic C3-group of sterol is required for proper orientation of the substrate C-methyl intermediate in the activated complex.
