4.2.1.83: 4-oxalomesaconate hydratase
This is an abbreviated version!
For detailed information about 4-oxalomesaconate hydratase, go to the full flat file.
Word Map on EC 4.2.1.83
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4.2.1.83
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ochraceae
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vanillate
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2-pyrone-4,6-dicarboxylate
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protocatechuate
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syringate
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lignin
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4,5-cleavage
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sphingomonas
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paucimobilis
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aldolase
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ecori
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4,5-dioxygenase
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ligab
- 4.2.1.83
- ochraceae
- vanillate
- 2-pyrone-4,6-dicarboxylate
- protocatechuate
- syringate
- lignin
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4,5-cleavage
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sphingomonas
- paucimobilis
- aldolase
- ecori
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4,5-dioxygenase
- ligab
Reaction
Synonyms
4-carboxy-2-oxobutane-1,2,4-tricarboxylate 2,3-hydro-lyase, 4-carboxy-2-oxohexenedioate hydratase, 4-oxalmesaconate hydratase, 4-oxalomesaconate hydratase, gamma-oxalomesaconate hydratase, hydratase, oxalmesaconate, LigJ, OMA, OMA hydratase, oxalmesaconate hydratase, PmdE, PocOMH
ECTree
Advanced search results
Engineering
Engineering on EC 4.2.1.83 - 4-oxalomesaconate hydratase
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C124S
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kcat/Km for 4-oxalomesaconate is 1.9fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C131S
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kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C183S
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kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C186S
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kcat/Km for 4-oxalomesaconate is 16% higher than wild-type value, mutant enzyme is more stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C205S
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kcat/Km for 4-oxalomesaconate is 29% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C260S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C92S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C96S
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kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
C131S
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kcat/Km for 4-oxalomesaconate is 26% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C183S
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kcat/Km for 4-oxalomesaconate is 1.8fold higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C260S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C92S
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kcat/Km for 4-oxalomesaconate is 18% higher than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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C96S
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kcat/Km for 4-oxalomesaconate is 3.9fold lower than wild-type value, mutant enzyme is less stable than wild-type enzyme at 4°C in 20 mM potassium phosphate buffer containing 1 mM DTT
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additional information
D0IZN8
generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
additional information
generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
additional information
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generation of several pmdE gene truncated mutants, lacking residues 6 to 226, 32 to 296, or 105 to 215, overview. A pmdE knock out mutant loses the ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate as carbon sources. This ability to grow on vanillate, 3-hydroxybenzoate, and 4-hydroxybenzoate is restored by genetic complementation
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