Reaction of o-aminophenyldiphenylmethanol with ?-acetylenic ketone

1993 ◽  
Vol 29 (10) ◽  
pp. 1232-1233
Author(s):  
T. P. Kosulina ◽  
E. V. Gromachevskaya ◽  
V. G. Kul'nevich
Keyword(s):  
Acetylenic Ketone

Synthesis of 14-hydroxy steroids. Total synthesis of methyl 14β-hydroxy-1,7,17-trioxo-5β,8-androstene-10β-oate and related compounds

1990 ◽  
Vol 68 (11) ◽  
pp. 1917-1922 ◽  
Author(s):  
Réjean Ruel ◽  
Pierre Deslongchamps
Keyword(s):  
Total Synthesis ◽  
Ammonium Salt ◽  
Michael Addition ◽  
Title Compound ◽  
Steroid Synthesis ◽  
Related Compounds ◽  
Acetylenic Ketone

The total synthesis of the title compound 22 and methyl 14α-hydroxy-5β,13α,8-androstene-1,7,17-trioxo-10β-oate 21 isomer is reported. We also describe the 1,6-Michael addition of 2-methyl-1,3-cyclopentanedione on dienone 14 and the protic ammonium salt catalyzed intramolecular Michael addition of cyclic β-ketoester on the conjugated acetylenic ketone 13. Keywords: cardenolides, steroid synthesis, aldol, Michael addition.

Synthesis and Characterization of Some New Cycloaddition Products of Bifunctional Acetylenic Ketone

2003 ◽  
Vol 33 (18) ◽  
pp. 3135-3146 ◽  
Author(s):  
R. K. Tiwari ◽  
A. K. Saxena
Keyword(s):  
Synthesis And Characterization ◽  
Acetylenic Ketone

Intramolecular Michael addition of cyclic β-ketoester on conjugated acetylenic ketone.

1986 ◽  
Vol 27 (45) ◽  
pp. 5455-5458 ◽  
Author(s):  
Jean-François Lavallée ◽  
Gilles Berthiaume ◽  
Pierre Deslongchamps ◽  
Fritz Grein
Keyword(s):  
Michael Addition ◽  
Acetylenic Ketone

ChemInform Abstract: PHOTOCHEMICAL Γ-HYDROGEN ABSTRACTION IN AN α-ACETYLENIC KETONE. COMPARISON WITH AN ANALOGOUS ENONE

1976 ◽  
Vol 7 (28) ◽  
pp. no-no
Author(s):  
PAUL S. ENGEL ◽  
MYRON E. SCHROEDER ◽  
MARY A. SCHEXNAYDER
Keyword(s):  
Hydrogen Abstraction ◽  
Acetylenic Ketone

The Addition of Malonic Esters to an Acetylenic Ketone

1950 ◽  
Vol 72 (2) ◽  
pp. 1022-1023 ◽  
Author(s):  
Charles L. Bickel
Keyword(s):  
Acetylenic Ketone

A rare example of extremely strong carbon—carbon coupling: Analysis of13C and1H NMR spectra of a13C2-acetylenic ketone

1987 ◽  
Vol 25 (5) ◽  
pp. 462-465 ◽  
Author(s):  
Richard J. Auchus ◽  
André d'Avignon ◽  
Douglas F. Covey
Keyword(s):  
Nmr Spectra ◽  
Coupling Analysis ◽  
Acetylenic Ketone

Note: A new acetylenic ketone from the bark of Litsea rotundifolia var. oblongifolia

2005 ◽  
Vol 7 (1) ◽  
pp. 75-79 ◽  
Author(s):  
Ya Zhao ◽  
Guo-Qiang Song ◽  
Yue-Wei Guo
Keyword(s):  
Acetylenic Ketone

scholarly journals Inactivation of Δ5-3-oxo steroid isomerase with active-site-directed acetylenic steroids

1981 ◽  
Vol 193 (1) ◽  
pp. 217-227 ◽  
Author(s):  
T M Penning ◽  
D F Covey ◽  
P Talalay
Keyword(s):  
Active Site ◽  
Competitive Inhibition ◽  
Enzyme Inhibitor ◽  
Covalent Bond ◽  
Addition Product ◽  
Ring Structure ◽  
Dependent Manner ◽  
Compound I ◽  
Inhibitor Complex ◽  
Acetylenic Ketone

Several steroid analogues containing conjugated acetylenic ketone groups as part of a seco-ring structure or as substituents on the intact steroid system are irreversible inhibitors of delta 5-3-oxo steroid isomerase (EC 5.3.3.1) from Pseudomonas testosteroni. Thus 10 beta-(1-oxoprop-2-ynyl)oestr-4-ene-3,17-dione (I), 5,10-seco-oestr-4-yne-3,10,17-trione (II), 17 beta-hydroxy-5,10-seco-oestr-4-yne-3,10-dione (III) and 17 beta-(1-oxoprop-2-ynyl)androst-4-en-3-one (IV) irreversibly inactivate isomerase in a time-dependent manner. In all cases saturation kinetics are observed. Protection against inactivation is afforded by the powerful competitive inhibitor 19-nortestosterone. The inhibition constants (Ki) for 19-nortestosterone obtained from such experiments are in good agreement with those determined from conventional competitive-inhibition studies of enzyme activity. These compounds thus appear to be active-site directed. In every case the inactivated enzyme could be dialysed without return of activity, indicating that a stable covalent bond probably had formed between the steroid and enzyme. Compound (I) is a very potent inhibitor of isomerase [Ki = 66.0 microM and k+2 = 12.5 × 10(-3) s-1 (where Ki is the dissociation constant of the reversible enzyme-inhibitor complex and k+2 is the rate constant for the inactivation reaction of the enzyme-inhibitor complex)] giving half-lives of inactivation of 30-45 s at saturation. It is argued that the basic-amino-acid residue that abstracts the intramolecularly transferred 4 beta-proton in the reaction mechanism could form a Michael-addition product with compound (I). In contrast, although compound (IV) has a lower inhibition constant (Ki = 14.5 microM), it is a relatively poor alkylating agent (k+2 = 0.13 × 10(-3) s-1). If the conjugated acetylenic ketone groups are replaced by alpha-hydroxyacetylene groups, the resultant analogues of steroids (I)-(IV) are reversible competitive inhibitors with Ki values in the range 27-350 microM. The enzyme binds steroids in the C19 series with functionalized acetylenic substituents at C-17 in preference to steroids in the C18 series bearing similar groups in the ring structure or as C-10 substituents. In the 5,10-seco-steroid series the presence of hydroxy groups at both C-3 and C-17 is deleterious to binding by the enzyme.

Dehydrogenase inactivation by an enzyme-generated acetylenic ketone: identification of a lysyl enaminone by carbon-13 NMR

1987 ◽  
Vol 109 (1) ◽  
pp. 280-282 ◽  
Author(s):  
Richard J. Auchus ◽  
Douglas F. Covey
Keyword(s):  
Acetylenic Ketone
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