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E134Q
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catalytic properties of the five different component enzyme activities of the alpha/Arg134Gln mutant complex show no significant changes as compared with those of the wild-type complex. In the alpha/Glu139Gln mutant complex DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase shows 60% decreased turnover number and a significant increase in Km for 3-cis-tetradecenoyl-CoA
E139Q
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The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
E136A
variant to study the importance of Glu136 for catalysis
E151X
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site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
E165Q
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site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
N211X
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site-directe mutagenesis of putative active-site amino acid residues. Exchange of Arg151 and Asp211 leads to a reduced expression of the recombinant enzyme accompanied by a reduced activity. The replacement of Glu165 by Gln leads to a strongly reduced enzymatic activity. Tyr150 is not involved in isomerase catalysis
F268A
the mutant shows reduced activity compared to the wild type enzyme
N101A
the mutant shows reduced activity compared to the wild type enzyme
R100A
the mutant shows reduced activity compared to the wild type enzyme
additional information
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in the absence of DELTA3,DELTA2-enoyl CoA isomerase, complete beta-oxidation of (10Z)-heptadecanoic acid is blocked. In vivo enzyme activity tests of the proteins encoded by AtECI1, AtECI2, and AtECI3 by complementation of the Saccharomyces cerevisiae double mutant eciDELTAdci1DELTA with deletions of the genes, DELTA2,DELTA3-enoyl-CoA isomerase and DELTA3,4,DELTA2,4-dienoyl CoA isomerase
D149E
decrease in catalytic activity
D149E
turnover number for trans-3-hexenoyl-CoA is 2.3fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242C
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 1.9 micromol per min and mg
K242C
turnover number for trans-3-hexenoyl-CoA is 14.5fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242C
turnover number for trans-3-hexenoyl-CoA is 160 fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme. Mutation allows DELTA3-DELTA2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity
K242D
decrease in catalytic activity, mutants shows slight additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.026 micromol per min and mg
K242D
turnover number for trans-3-hexenoyl-CoA is 12308fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242D
turnover number for trans-3-hexenoyl-CoA is 2667fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242F
decrease in catalytic activity
K242F
turnover number for trans-3-hexenoyl-CoA is 1143fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242R
decrease in catalytic activity
K242R
turnover number for trans-3-hexenoyl-CoA is 3.2fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242T
decrease in catalytic activity, mutants shows additional hydratase activity on 2-hexenoyl-CoA with Vmax of 0.041 micromol per min and mg
K242T
turnover number for trans-3-hexenoyl-CoA is 7619fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme
K242T
turnover number for trans-3-hexenoyl-CoA is 842fold lower than wild-type value, Km-value for trans-3-hexenoyl-CoA is fold higher than wild-type enzyme