Cytochrome P450 subfamily CYP710A genes encode sterol C-22 desaturase in plants

2006 ◽  
Vol 34 (6) ◽  
pp. 1202-1205 ◽  
Author(s):  
T. Morikawa ◽  
M. Mizutani ◽  
D. Ohta
Keyword(s):  
Cytochrome P450 ◽  
Double Bond ◽  
Steroid Hormones ◽  
Plant Sterol ◽  
Biosynthetic Pathway ◽  
Mevalonate Pathway ◽  
Membrane Integrity ◽  
The Other ◽  
Side Chain ◽  
Cellular Functions

Sterols are isoprenoid-derived lipids that are produced via the mevalonate pathway and are involved in various cellular functions in eukaryotes such as maintenance of membrane integrity and biosynthetic precursors of steroid hormones. Among cellular sterols, Δ22-sterols containing a double bond at C-22 in the sterol side chain specifically occur in fungi (ergosterol) and plants (stigmasterol and brassicasterol), and several lines of experimental evidence have suggested specific physiological roles of Δ22-sterols in plants. Fungal cytochrome P450 (P450), CYP61, has been established as the sterol C-22 desaturase functioning at the penultimate step in the ergosterol biosynthetic pathway. On the other hand, no particular sequence has been assigned as to the enzyme responsible for the introduction of the double bond into the sterol side chain in plants. In this review, we summarize our recent findings demonstrating that CYP710A P450 family genes encode the plant sterol C-22 desaturases to produce stigmasterol and brassicasterol/crinosterol from β-sitosterol and 24-epi-campesterol respectively.

scholarly journals Oxepinamide F biosynthesis involves enzymatic d-aminoacyl epimerization, 3H-oxepin formation, and hydroxylation induced double bond migration

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Liujuan Zheng ◽  
Haowen Wang ◽  
Aili Fan ◽  
Shu-Ming Li
Keyword(s):  
Cytochrome P450 ◽  
Double Bond ◽  
Biosynthetic Pathway ◽  
Hydroxyl Group ◽  
Cytochrome P450 Enzyme ◽  
Double Bond Migration ◽  
Feeding Experiments ◽  
Aspergillus Ustus ◽  
P450 Enzyme ◽  
Derivatives Of

Abstract Oxepinamides are derivatives of anthranilyl-containing tripeptides and share an oxepin ring and a fused pyrimidinone moiety. To the best of our knowledge, no studies have been reported on the elucidation of an oxepinamide biosynthetic pathway and conversion of a quinazolinone to a pyrimidinone-fused 1H-oxepin framework by a cytochrome P450 enzyme in fungal natural product biosynthesis. Here we report the isolation of oxepinamide F from Aspergillus ustus and identification of its biosynthetic pathway by gene deletion, heterologous expression, feeding experiments, and enzyme assays. The nonribosomal peptide synthase (NRPS) OpaA assembles the quinazolinone core with d-Phe incorporation. The cytochrome P450 enzyme OpaB catalyzes alone the oxepin ring formation. The flavoenzyme OpaC installs subsequently one hydroxyl group at the oxepin ring, accompanied by double bond migration. The epimerase OpaE changes the d-Phe residue back to l-form, which is essential for the final methylation by OpaF.

scholarly journals Effects of mrpigG on Development and Secondary Metabolism of Monascus ruber M7

2020 ◽  
Vol 6 (3) ◽  
pp. 156
Author(s):  
Li Li ◽  
Fusheng Chen
Keyword(s):  
Biosynthetic Pathway ◽  
Gene Deletion ◽  
The Other ◽  
Side Chain ◽  
Asian Countries ◽  
Monascus Ruber ◽  
Monascus Pigments ◽  
The World ◽  
Carbon Side Chain ◽  
Yellow Pigments

Monascus pigments (MPs) have been used as food colorants for several centuries in Asian countries and are now used throughout the world via Asian catering. The MP biosynthetic pathway has been well-illustrated, but the functions of a few genes, including mrpigG, in the MP gene cluster are still unclear. In the current study, in order to investigate the function of mrpigG in M. ruber M7, gene deletion (ΔmrpigG), complementation (ΔmrpigG::mrpigG) and overexpression (M7::PtrpC-mrpigG) mutants were successfully obtained. The morphologies and biomasses, as well as the MP and citrinin production, of these mutants were analyzed. The results revealed that the disruption, complementation and overexpression of mrpigG showed no apparent defects in morphology, biomass or citrinin production (except MP production) in ΔmrpigG compared with M. ruber M7. Although the MP profiles of ΔmrpigG and M. ruber M7 were almost the same—with both having four yellow pigments, two orange pigments (OPs) and two red pigments (RPs)—their yields were decreased in ΔmrpigG to a certain extent. Particularly, the content of rubropunctatin (an OP) and its derivative rubropunctamine (an RP) in ΔmrpigG, both of which have a five-carbon side chain, accounted for 57.7%, and 22.3% of those in M. ruber M7. On the other hand, monascorubrin (an OP) and its derivative monascorubramine (an RP), both of which have a seven-carbon side chain, were increased by 1.15 and 2.55 times, respectively, in ΔmrpigG compared with M. ruber M7. These results suggest that the MrPigG protein may preferentially catalyze the biosynthesis of MPs with a five-carbon side chain.

scholarly journals Substrate specificity of two cytochrome P450 monooxygenases involved in lankamycin biosynthesis

2021 ◽  
Vol 85 (1) ◽  
pp. 115-125
Author(s):  
Aiko Teshima ◽  
Hisashi Kondo ◽  
Yu Tanaka ◽  
Yosi Nindita ◽  
Yuya Misaki ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cytochrome P450 ◽  
Substrate Specificity ◽  
Double Mutant ◽  
Biosynthetic Pathway ◽  
Substrate Recognition ◽  
Streptomyces Lividans ◽  
The Other ◽  
Cytochrome P450 Monooxygenases ◽  
P450 Monooxygenases

Abstract To elucidate the gross lankamycin biosynthetic pathway including two cytochrome P450 monooxygenases, LkmK and LkmF, we constructed two double mutants of P450 genes in combination with glycosyltransferase genes, lkmL and lkmI. An aglycon 8,15-dideoxylankanolide, a possible substrate for LkmK, was prepared from an lkmK–lkmL double mutant, while a monoglycoside 3-O-l-arcanosyl-8-deoxylankanolide, a substrate for LkmF, was from an lkmF–lkmI double mutant. Bioconversion of lankamycin derivatives was performed in the Escherichia coli recombinant for LkmK and the Streptomyces lividans recombinant for LkmF, respectively. LkmK catalyzes the C-15 hydroxylation on all 15-deoxy derivatives, including 8,15-dideoxylankanolide (a possible substrate), 8,15-dideoxylankamycin, and 15-deoxylankamycin, suggesting the relaxed substrate specificity of LkmK. On the other hand, LkmF hydroxylates the C-8 methine of 3-O-l-anosyl-8-deoxylankanolide. Other 8-deoxy lankamycin/lankanolide derivatives were not oxidized, suggesting the importance of a C-3 l-arcanosyl moiety for substrate recognition by LkmF in lankamycin biosynthesis. Thus, LkmF has a strict substrate specificity in lankamycin biosynthesis.

A Novel Scheme for the Synthesis of 21-Acetoxypregna-1,4,9(11)-triene- 17α,21-diol-3,20-dione from 9α-Hydroxyandrostenedione

2020 ◽  
Vol 16 (5) ◽  
pp. 606-610
Author(s):  
Nguyen T. Diep ◽  
Luu D. Huy
Keyword(s):  
Double Bond ◽  
Chemical Synthesis ◽  
Economic Efficiency ◽  
Final Stage ◽  
Side Chain ◽  
Entire Process ◽  
Drug Synthesis ◽  
First Time

Background: Vietnam currently imports up to 90% of the pharmaceuticals it consumes and 100% of the steroid-based pharmaceuticals. The ability for efficient chemical synthesis of the steroids could create commercial opportunities to address this issue. Synthesis of 21-acetoxypregna-1,4,9(11)- triene-17α,21-diol-3,20-dione is considered a key intermediate in the scheme of steroidal drug synthesis. Previous synthesis attempts of such steroids (corticoids) introduce a double bond at C-1(2) in the final stage of synthesis, which delivers a poor yield and reduces the economic efficiency of the process. Objective: To study and develop a novel and effective method for the synthesis of 21-acetoxypregna- 1,4,9(11)-triene-17α,21-diol-3,20-dione. Methods: Using 9α-hydroxyandrostenedione as a substrate chemical synthesis was performed as follows: pregnane side chain construction at C-17 (acetylene method), introduction of C-1(2) double bond (using SeO2), epimerization of C-17 (via 17-ONO2 ester) and Stork’s iodination. Results: 21-acetoxypregna-1,4,9(11)-triene-17α,21-diol-3,20-dione was prepared from 9α- hydroxyandrostenedione with an improved yield compared to previous attempts. Conclusion: Here, 21-acetoxypregna-1,4,9(11)-triene-17α,21-diol-3,20-dione has been synthesized from 9α-hydroxyandrostenedione based on a novel, effective and commercially feasible scheme. The introduction of the C-1(2) double bond at an earlier stage of the synthesis has increased the economic efficiency of the entire process. For the first time, the indirect epimerization mechanism has been clarified along with the configuration of the C-17 stereo-center which has been confirmed using NOESY data.

Comparison of the Potency of 8-L-Arginine, 8-D-Arginine and 8-D-Homoarginine Vasopressin Analogs with Substituted Phenylalanine in Position 2

1994 ◽  
Vol 59 (6) ◽  
pp. 1439-1450 ◽  
Author(s):  
Miroslava Žertová ◽  
Jiřina Slaninová ◽  
Zdenko Procházka
Keyword(s):  
Amino Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Basic Amino Acid ◽  
The Other ◽  
Side Chain ◽  
Inhibitory Potency ◽  
Phase Synthesis ◽  
Other Hand ◽  
Order Of Magnitude

An analysis of the uterotonic potencies of all analogs having substituted L- or D-tyrosine or -phenylalanine in position 2 and L-arginine, D-arginine or D-homoarginine in position 8 was made. The series of analogs already published was completed by the solid phase synthesis of ten new analogs having L- or D-Phe, L- or D-Phe(2-Et), L- or D-Phe(2,4,6-triMe) or D-Tyr(Me) in position 2 and either L- or D-arginine in position 8. All newly synthesized analogs were found to be uterotonic inhibitors. Deamination increases both the agonistic and antagonistic potency. In the case of phenylalanine analogs the change of configuration from L to D in position 2 enhances the uterotonic inhibition for more than 1 order of magnitude. The L to D change in position 8 enhances the inhibitory potency negligibly. Prolongation of the side chain of the D-basic amino acid in position 8 seems to decrease slightly the inhibitory potency if there is L-substituted amino acid in position 2. On the other hand there is a tendency to the increase of the inhibitory potency if there is D-substituted amino acid in position 2.

scholarly journals Effect of Temperature on the Corrosion Inhibition of Trans-4-Hydroxy-4′-Stilbazole on Mild Steel in HCl Solution

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Ayssar Nahlé ◽  
Ideisan I. Abu-Abdoun ◽  
Ibrahim Abdel-Rahman
Keyword(s):  
Weight Loss ◽  
Double Bond ◽  
Adsorption Isotherm ◽  
Mild Steel ◽  
Corrosion Inhibitor ◽  
Thermodynamic Parameters ◽  
The Other ◽  
Effect Of Temperature ◽  
Temkin Adsorption Isotherm ◽  
Hcl Solution

The inhibition and the effect of temperature and concentration of trans-4-hydroxy-4′-stilbazole on the corrosion of mild steel in 1 M HCl solution was investigated by weight loss experiments at temperatures ranging from 303 to 343 K. The studied inhibitor concentrations were between  M and  M. The percentage inhibition increased with the increase of the concentration of the inhibitor. The percentage inhibition reached about 94% at the concentration of  M and 303 K. On the other hand, the percentage inhibition decreased with the increase of temperature. Using the Temkin adsorption isotherm, the thermodynamic parameters for the adsorption of this inhibitor on the metal surface were calculated. Trans-4-hydroxy-4′-stilbazole was found to be a potential corrosion inhibitor since it contained not only nitrogen and oxygen, but also phenyl and pyridine rings that are joined together with a double bond (–C=C–) in conjugation with these rings.

Structural Studies on N-(2,4,6-Trimethylphenyl)-methyl/ chloro-acetamides, 2,4,6-(CH3)3C6H2NH-CO-CH3–yXy (X = CH3 or Cl and y = 0, 1, 2)

2006 ◽  
Vol 61 (10-11) ◽  
pp. 588-594 ◽  
Author(s):  
Basavalinganadoddy Thimme Gowda ◽  
Jozef Kožíšek ◽  
Hartmut Fuess
Keyword(s):  
Crystal Structure ◽  
Crystal Structures ◽  
Structural Data ◽  
The Other ◽  
Side Chain ◽  
Structural Studies ◽  
Asymmetric Unit ◽  
Lattice Constants ◽  
Peptide Linkage ◽  
The Mean

TMPAThe effect of substitutions in the ring and in the side chain on the crystal structure of N- (2,4,6-trimethylphenyl)-methyl/chloro-acetamides of the configuration 2,4,6-(CH3)3C6H2NH-COCH3− yXy (X = CH3 or Cl and y = 0,1, 2) has been studied by determining the crystal structures of N-(2,4,6-trimethylphenyl)-acetamide, 2,4,6-(CH3)3C6H2NH-CO-CH3 (); N-(2,4,6- trimethylphenyl)-2-methylacetamide, 2,4,6-(CH3)3C6H2NH-CO-CH2-CH3 (TMPMA); N-(2,4,6- trimethylphenyl)-2,2-dimethylacetamide, 2,4,6-(CH3)3C6H2NH-CO-CH(CH3)2 (TMPDMA) and N-(2,4,6-trimethylphenyl)-2,2-dichloroacetamide, 2,4,6-(CH3)3C6H2NH-CO-CHCl2 (TMPDCA). The crystallographic system, space group, formula units and lattice constants in Å are: TMPA: monoclinic, Pn, Z = 2, a = 8.142(3), b = 8.469(3), c = 8.223(3), β = 113.61(2)◦; TMPMA: monoclinic, P21/n, Z = 8, a = 9.103(1), b = 15.812(2), c = 16.4787(19), α = 89.974(10)◦, β = 96.951(10)◦, γ =89.967(10)◦; TMPDMA: monoclinic, P21/c, Z = 4, a =4.757(1), b= 24.644(4), c =10.785(2), β = 99.647(17)◦; TMPDCA: triclinic, P¯1, Z = 2, a = 4.652(1), b = 11.006(1), c = 12.369(1), α = 82.521(7)◦, β = 83.09(1)◦, γ = 79.84(1)◦. The results are analyzed along with the structural data of N-phenylacetamide, C6H5NH-CO-CH3; N-(2,4,6-trimethylphenyl)-2-chloroacetamide, 2,4,6-(CH3)3C6H2NH-CO-CH2Cl; N-(2,4,6-trichlorophenyl)-acetamide, 2,4,6-Cl3C6H2NH-COCH3; N-(2,4,6-trichlorophenyl)-2-chloroacetamide, 2,4,6-Cl3C6H2NH-CO-CH2Cl; N-(2,4,6-trichlorophenyl)- 2,2-dichloroacetamide, 2,4,6-Cl3C6H2NH-CO-CHCl2 and N-(2,4,6-trichlorophenyl)- 2,2,2-trichloroacetamide, 2,4,6-Cl3C6H2NH-CO-CCl3. TMPA, TMPMA and TMPDCA have one molecule each in their asymmetric units, while TMPDMA has two molecules in its asymmetric unit. Changes in the mean ring distances are smaller on substitution as the effect has to be transmitted through the peptide linkage. The comparison of the other bond parameters reveal that there are significant changes in them on substitution.

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