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Literature summary extracted from

  • Taylor, K.L.; Xiang, H.; Liu, R.Q.; Yang, G.; Dunaway-Mariano, D.
    Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A dehalogenase (1997), Biochemistry, 36, 1349-1361.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.8.1.7 D145A mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption Pseudomonas sp.
3.8.1.7 F64L The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift Pseudomonas sp.
3.8.1.7 F82L The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift Pseudomonas sp.
3.8.1.7 G114A The G114A mutant is strongly inhibited in both substrate binding and activation Pseudomonas sp.
3.8.1.7 H90Q mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption Pseudomonas sp.
3.8.1.7 W89F The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift Pseudomonas sp.
3.8.1.7 W89Y The W89Y mutant is inhibited in catalysis and ligand binding Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.8.1.7 Pseudomonas sp.
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3.8.1.7 Pseudomonas sp.
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wild-type and mutant enzymes D145A, H90Q, W137F, W89F, W89Y, F64L, F82L, G114A
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3.8.1.7 Pseudomonas sp. CBS-3
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