scholarly journals Mitochondrial metabolism of 3-mercaptopropionic acid. Chemical synthesis of 3-mercaptopropionyl coenzyme A and some of its S-acyl derivatives.

1985 ◽  
Vol 260 (12) ◽  
pp. 7330-7336
Author(s):  
D Cuebas ◽  
J D Beckmann ◽  
F E Frerman ◽  
H Schulz
Keyword(s):  
Chemical Synthesis ◽  
Coenzyme A ◽  
Mitochondrial Metabolism ◽  
Mercaptopropionic Acid ◽  
Acyl Derivatives

Chemical synthesis of β-ketooctanoyl coenzyme A

1960 ◽  
Vol 1 (1) ◽  
pp. 8-16 ◽  
Author(s):  
P.Roy Vagelos ◽  
A.W. Alberts
Keyword(s):  
Chemical Synthesis ◽  
Coenzyme A

scholarly journals An enhanced chemoenzymatic method for loading substrates onto carrier protein domains

2018 ◽  
Vol 96 (3) ◽  
pp. 372-379 ◽  
Author(s):  
Tiia Kittilä ◽  
Max J. Cryle
Keyword(s):  
Chemical Synthesis ◽  
Coenzyme A ◽  
Carrier Protein ◽  
Crucial Importance ◽  
Carrier Proteins ◽  
Improved Method ◽  
One Pot ◽  
Loading Method ◽  
Peptide Synthetase ◽  
New Compounds

Non-ribosomal peptide synthetase (NRPS) machineries produce many medically relevant peptides that cannot be easily accessed by chemical synthesis. Thus, understanding NRPS mechanism is of crucial importance to allow efficient redesign of these machineries to produce new compounds. During NRPS-mediated synthesis, substrates are covalently attached to peptidyl carrier proteins (PCPs), and studies of NRPSs are impeded by difficulties in producing PCPs loaded with substrates. Different approaches to load substrates onto PCP domains have been described, but all suffer from difficulties in either the complexity of chemical synthesis or low enzymatic efficiency. Here, we describe an enhanced chemoenzymatic loading method that combines 2 approaches into a single, highly efficient one-pot loading reaction. First, d-pantetheine and ATP are converted into dephospho-coenzyme A via the actions of 2 enzymes from coenzyme A (CoA) biosynthesis. Next, phosphoadenylates are dephosphorylated using alkaline phosphatase to allow linker attachment to PCP domain by Sfp mutant R4-4, which is inhibited by phosphoadenylates. This route does not depend on activity of the commonly problematic dephospho-CoA kinase and, therefore, offers an improved method for substrate loading onto PCP domains.

Chemical Synthesis of Tropoyl Coenzyme A

1980 ◽  
Vol 35 (5-6) ◽  
pp. 363-366 ◽  
Author(s):  
Georg G. Gross ◽  
Karl J. Koelen
Keyword(s):  
Chemical Synthesis ◽  
Extinction Coefficient ◽  
Alkaline Hydrolysis ◽  
Absorption Maximum ◽  
Coenzyme A ◽  
Difference Spectrum ◽  
Uv Spectrum ◽  
Negative Results ◽  
Thioester Bond ◽  
Hydrolysis Of

Abstract Tropoyl coenzyme A has been synthesized in good yields via the corresponding N-hydroxysuc-cinimide ester. The UV-spectrum of the purified thioester has an absorption maximum at 257 nm; at this wavelength, a molar extinction coefficient of 19.2 × 106 [cm2 mol-1] has been determined. Upon alkaline hydrolysis of the thioester bond a difference spectrum with Amax at 235 nm (Δe235= 4.8 × 106 [cm2 mol-1]) has been observed. Attempts to prepare 2-phenylmalonyl coenzyme A by the same technique gave negative results.

First total chemical synthesis of natural acyl derivatives of some phenolglycosides of the family Salicaceae

2012 ◽  
Vol 363 ◽  
pp. 66-72 ◽  
Author(s):  
Maxim L. Belyanin ◽  
Elena V. Stepanova ◽  
Vladimir D. Ogorodnikov
Keyword(s):  
Chemical Synthesis ◽  
The Family ◽  
Derivatives Of ◽  
Acyl Derivatives

scholarly journals On the Mechanism of Dehydrogenation of Fatty Acyl Derivatives of Coenzyme A

1958 ◽  
Vol 233 (4) ◽  
pp. 843-852 ◽  
Author(s):  
Elizabeth P. Steyn-Parvé ◽  
Helmut Beinert
Keyword(s):  
Coenzyme A ◽  
Fatty Acyl ◽  
Derivatives Of ◽  
Acyl Derivatives

scholarly journals ON THE MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME A

1956 ◽  
Vol 218 (2) ◽  
pp. 701-716 ◽  
Author(s):  
F.L. Crane ◽  
S. Mii ◽  
Jens G. Hauge ◽  
D.E. Green ◽  
Helmut Beinert
Keyword(s):  
Coenzyme A ◽  
Fatty Acyl ◽  
Derivatives Of ◽  
Acyl Derivatives
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