2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase
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For detailed information about cyclopropane-fatty-acyl-phospholipid synthase, go to the full flat file.
Reaction
Synonyms
C17:cyclopropane synthase, Cfa, CFA synthase, cfaB, CFAS, CPS, CPS1, CPS2, CPS3, cyclopropane fatty acid synthase, cyclopropane fatty acid synthetase, cyclopropane fatty acyl synthase, cyclopropane synthase, cyclopropane-fatty-acyl-phospholipid synthase, HP0416, SfCPA-FAS, synthetase, cyclopropane fatty acid, unsaturated-phospholipid methyltransferase
ECTree
2.1.1.79 cyclopropane-fatty-acyl-phospholipid synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.1.1.79 - cyclopropane-fatty-acyl-phospholipid synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C139S
E239A
G236E
H266A
Y317F
C139S
-
mutant retains 31% of the activity of the wild-type enzyme. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 85% of wild-type activity
G236E
the mutant has less than 1% of the in vitro activity of the wild type enzyme. The reaction catalyzed by this G236E mutant starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively
G236E
active site mutant, replacing the strictly conserved G236 by a glutamate residue, which corresponds to E146 of the homologous mycolic acid methyltransferase. Mutant has less than 1% of the in vitro activity of the wild-type enzyme and leads to the formation of cyclopropanated fatty acid methyl esters and of new C17 methyl-branched unsaturated fatty acid methyl esters. The double bond of the latters is located at different positions 8, 9 or 10, and the methyl group at position 10 or 9. The reaction catalyzed by G236E mutant thus starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively. It follows then two competing steps, a normal cyclopropanation or hydride shift/elimination events giving different combinations of alkenes
H266A
-
catalytic efficiency is 5.3% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 16% of wild-type activity
Y317F
-
catalytic efficiency is 0.7% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 14% of wild-type activity
