2006
DOI: 10.1002/bit.20910
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Influence of global fluorination on chloramphenicol acetyltransferase activity and stability

Abstract: Varied levels of fluorinated amino acid have been introduced biosynthetically to test the functional limits of global substitution on enzymatic activity and stability. Replacement of all the leucine (LEU) residues in the enzyme chloramphenicol acetyltransferase (CAT) with the analog, 5',5',5'-trifluoroleucine (TFL), results in the maintenance of enzymatic activity under ambient temperatures as well as an enhancement in secondary structure but loss in stability against heat and denaturants or organic co-solvent… Show more

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Cited by 34 publications
(41 citation statements)
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“…Replacement of all the leucine residues by 5′,5′,5′-trifluoroleucines in the enzyme chloramphenicol acetyltransferase (CAT) preserved enzymatic activity at an ambient temperature as well as an enhancement in secondary structure [112]. However, chemical and thermal destabilizations were noted at elevated temperature that increased with increased trifluoroleucine incorporation.…”
Section: Amino Acids and Proteins With Fluorinated Patchesmentioning
confidence: 95%
See 1 more Smart Citation
“…Replacement of all the leucine residues by 5′,5′,5′-trifluoroleucines in the enzyme chloramphenicol acetyltransferase (CAT) preserved enzymatic activity at an ambient temperature as well as an enhancement in secondary structure [112]. However, chemical and thermal destabilizations were noted at elevated temperature that increased with increased trifluoroleucine incorporation.…”
Section: Amino Acids and Proteins With Fluorinated Patchesmentioning
confidence: 95%
“…Yet, remarkably, many studies indicate that in spite of notable changes related to the differences in steric demand, polarizability and electronegativity between CF 3 and CH 3 groups, and modifications in dipole moments and surface activity, substantially fluorinated proteins often retain the structure and activity of their native model [112][113][114]. Incorporation of trifluoromethyl alanine and other fluorinated amino acids in small chemotactic peptides preserved some of their aptitude at stimulating chemiluminescence in neutrophil cells [115].…”
Section: Amino Acids and Proteins With Fluorinated Patchesmentioning
confidence: 98%
“…As far as DfeGly and TfeGly are concerned, increasing degrees of fluorination apparently decrease the rate of coiled‐coil association. Although still awaiting direct experimental proof, we6a and others11 have proposed that this effect may be attributed to fluorine–fluorine contacts in the unfolded state. The assumption is that these contacts lead to an arrangement of the peptides that is inconsistent with correct folding and thus compete with structure formation.…”
Section: Methodsmentioning
confidence: 87%
“…Many functional groups including alkyne, alkene, ketone, and azides have been incorporated into the proteins via NAA, providing an orthogonal handle for protein modifications [122,223,224]. Halogenated NAAs, especially fluorinated amino acids, have made a significant impact on protein engineering [133,155,[225][226][227][228][229][230][231][232]. Repetitive protein polymers with fluorinated amino acid have shown distinct physicochemical properties, including an increase in thermal and chemical stability [155,228], as a result of the electronegativity and hydrophobicity of the fluorine atom [233,234].…”
Section: Modulating the Physicochemical Properties Of Protein Polymermentioning
confidence: 99%