Amiaspochalasins A–H, Undescribed Aspochalasins with a C-21 Ester Carbonyl from Aspergillus micronesiensis

2019 ◽  
Vol 84 (9) ◽  
pp. 5483-5491 ◽  
Author(s):  
Zhaodi Wu ◽  
Xiaotian Zhang ◽  
Weaam Hasan Al Anbari ◽  
Mi Zhang ◽  
Xia Chen ◽  
...  
Keyword(s):  
2014 ◽  
Vol 70 (11) ◽  
pp. 1050-1053 ◽  
Author(s):  
Xiang Li ◽  
Zhi-Gang Wang ◽  
Hou-He Chen ◽  
Sheng-Gao Liu

The title compound, C18H28O3, was prepared by the reaction of 2,6-di-tert-butylphenol with methyl acrylate under basic conditions using dimethyl sulfoxide as the promoter. The structure of this antioxidant indicates significant strain between theortho tert-butyl substituents and the phenolic OH group. In spite of the steric crowding of the OH group, it participates in intermolecular hydrogen bonding with the ester carbonyl O atom.


ChemInform ◽  
1987 ◽  
Vol 18 (52) ◽  
Author(s):  
G. VERARDO ◽  
P. STRAZZOLINI ◽  
A. G. GIUMANINI

1987 ◽  
Vol 28 (26) ◽  
pp. 3011-3012 ◽  
Author(s):  
Giancarlo Verardo ◽  
Paolo Strazzolini ◽  
Angelo G. Giumanini

1958 ◽  
Vol 36 (1) ◽  
pp. 151-158 ◽  
Author(s):  
R. A. Abramovitch

The infrared spectra of a number of malonate esters have been examined. Most of them exhibit two ester carbonyl stretching bands which have been shown not to be due to enolization and conjugate chelation or to association. The influence of α-substituents is discussed, as well as the reason for the splitting of the band.


Author(s):  
Mikhail S. Novikov ◽  
Igor V. Voznyi ◽  
Alexander F. Khlebnikov ◽  
Jürgen Kopf ◽  
Rafael R. Kostikov

1988 ◽  
Vol 53 (14) ◽  
pp. 3321-3325 ◽  
Author(s):  
Paolo Strazzolini ◽  
Giancarlo Verardo ◽  
Angelo G. Giumanini

1995 ◽  
Vol 307 (2) ◽  
pp. 335-339 ◽  
Author(s):  
J Grandchamps ◽  
M Nguyen-Distèche ◽  
C Damblon ◽  
J M Frère ◽  
J M Ghuysen

The Streptomyces K15 transferase is a penicillin-binding protein presumed to be involved in bacterial wall peptidoglycan crosslinking. It catalyses cleavage of the peptide, thiol ester or ester bond of carbonyl donors Z-R1-CONH-CHR2-COX-CHR3-COO- (where X is NH, S or O) and transfers the electrophilic group Z-R1-CONH-CHR2-CO to amino acceptors via an acyl-enzyme intermediate. Kinetic data suggest that the amino acceptor behaves as a simple alternative nucleophile at the level of the acyl-enzyme in the case of thiol ester and ester donors, and that it binds to the enzyme.carbonyl donor Michaelis complex and influences the rate of enzyme acylation by the carbonyl donor in the case of amide donors. Depending on the nature of the scissile bond, the enzyme has different requirements for substituents at positions R1, R2 and R3.


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