5.1.1.20: L-Ala-D/L-Glu epimerase
This is an abbreviated version!
For detailed information about L-Ala-D/L-Glu epimerase, go to the full flat file.
Reaction
Synonyms
AE epimerase, AEE, L-Ala-D/L-Glu epimerase, YcjG, YfkA, YfkB, YkfB
ECTree
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Engineering
Engineering on EC 5.1.1.20 - L-Ala-D/L-Glu epimerase
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D297G
I19A/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19C/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19F/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19L/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19N/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19S/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19T/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19V/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19W/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
I19Y/D297G
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the mutant enzyme shows o-succinylbenzoate synthase activity. Substitutions for Ile19 increases the growth rate relative to that for the D297G progenitor
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the mutant enzyme shows o-succinylbenzoate synthase activity at low level that is sufficient to permit anaerobic growth by an o-succinylbenzoate synthase-deficient strain of Escherichia coli, wild-type enzyme show
D297G
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the mutation is located at the end of the eighth beta-strand of the (beta/alpha)8-barrel. The mutant enzyme has no detectable muconate lactonizing activity. The mutant enzyme catalyzes the o-succinylbenzoate synthase reaction