Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides

1984 ◽  
Vol 230 (1) ◽  
pp. 117-128 ◽  
Author(s):  
A.J. Poulose ◽  
R.F. Bonsall ◽  
P.E. Kolattukudy
Keyword(s):  
Fatty Acid ◽  
Primary Structure ◽  
Active Site ◽  
Fatty Acid Synthase ◽  
Specific Modification ◽  
Condensation Domain

Escherichia coliCyclopropane Fatty Acid Synthase:  Is a Bound Bicarbonate Ion the Active-Site Base?†

Biochemistry ◽  
2005 ◽  
Vol 44 (41) ◽  
pp. 13583-13590 ◽  
Author(s):  
Fabienne Courtois ◽  
Olivier Ploux
Keyword(s):  
Fatty Acid ◽  
Active Site ◽  
Fatty Acid Synthase

scholarly journals Dibromopropanone Cross-linking of the Phosphopantetheine and Active-site Cysteine Thiols of the Animal Fatty Acid Synthase Can Occur Both Inter- and Intrasubunit

1999 ◽  
Vol 274 (17) ◽  
pp. 11557-11563 ◽  
Author(s):  
Andrzej Witkowski ◽  
Anil K. Joshi ◽  
Vangipuram S. Rangan ◽  
Arnold M. Falick ◽  
H. Ewa Witkowska ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Active Site ◽  
Fatty Acid Synthase ◽  
Cross Linking ◽  
Active Site Cysteine ◽  
Cysteine Thiols

scholarly journals In Silico Structure Prediction of Human Fatty Acid Synthase–Dehydratase: A Plausible Model for Understanding Active Site Interactions

2016 ◽  
Vol 10 ◽  
pp. BBI.S38317 ◽  
Author(s):  
Arun John ◽  
Vetrivel Umashankar ◽  
A. Samdani ◽  
Manoharan Sangeetha ◽  
Subramanian Krishnakumar ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Active Site ◽  
In Silico ◽  
Structure Prediction ◽  
Fatty Acid Synthase ◽  
Plausible Model

Active site directed inactivation of rat mammary gland fatty acid synthase by 3-chloropropionyl coenzyme A

Biochemistry ◽  
1986 ◽  
Vol 25 (2) ◽  
pp. 468-473 ◽  
Author(s):  
Henry M. Miziorko ◽  
Christine E. Behnke ◽  
Patricia M. Ahmad ◽  
Fazal Ahmad
Keyword(s):  
Mammary Gland ◽  
Fatty Acid ◽  
Active Site ◽  
Fatty Acid Synthase ◽  
Coenzyme A ◽  
Rat Mammary Gland

scholarly journals Characterization of fatty acid synthase monomers restrained from reassociating by immobilization to a solid support

1993 ◽  
Vol 292 (2) ◽  
pp. 361-364 ◽  
Author(s):  
J R Petithory ◽  
S Smith
Keyword(s):  
Fatty Acid ◽  
Active Site ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Solid Support ◽  
Protein Domain ◽  
Serine Residue ◽  
Subunit Dissociation ◽  
Per Se

The controversial question as to whether the ketoreductase activity of the animal fatty acid synthase is lost on dissociation of the homodimer has been addressed by using immobilized subunits which cannot reassociate under the conditions of assay. Ketoreductase activity, assessed with the model substrate S-acetoacetyl-N-acetylcysteamine, was identical in immobilized monomers and dimers, exhibiting normal Michaelis-Menten kinetics with Km values in the millimolar range. When acetoacetyl-CoA was used as a substrate, however, biphasic kinetics were observed in the case of the dimer, with estimated Km values in the micro- and milli-molar ranges, but only the high-Km reaction was observed with the monomer. Thus when the ketoreductase activities of the monomer and dimer are assessed with acetoacetyl-CoA at concentrations sufficient to saturate only the low-Km reaction, it appears that the ketoreductase activity towards acetoacetyl-CoA is lost upon dissociation. Reduction of acetoacetyl-CoA via the low-Km pathway is CoA-dependent, indicating that acetoacetyl-CoA can react with the dimer by two mechanisms: a high-Km pathway analogous to that utilized by model substrates and a low-Km pathway in which substrate and product are transferred between acyl-CoA and acyl-enzyme forms. The results indicate that the ketoreductase activity per se is unaffected by subunit dissociation and are consistent with a model in which the transfer of substrate from CoA ester to the acyl-carrier-protein domain necessitates juxtaposition of the transferase active-site serine residue of one subunit and the phosphopantetheine moiety of the adjacent subunit.

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