4.2.1.42: galactarate dehydratase
This is an abbreviated version!
For detailed information about galactarate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.42
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4.2.1.42
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enolase
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dehydration
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racemase
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mandelate
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departure
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agrobacterium
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alpha-proton
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aldolase
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dyad
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beta-strands
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glycerate
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d-galacturonate
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analysis
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seventh
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epimerization
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typhimurium
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semialdehyde
- 4.2.1.42
- enolase
- dehydration
- racemase
- mandelate
-
departure
-
agrobacterium
-
alpha-proton
- aldolase
-
dyad
-
beta-strands
- glycerate
- d-galacturonate
- analysis
-
seventh
-
epimerization
- typhimurium
- semialdehyde
Reaction
Synonyms
A9CG74, Dehydratase, galactarate, Galactarate dehydrase, galactarate dehydratase, galactarate dehydratase III, GalcD, GalrD, GalrD-III, L-talarate/galactarate dehydratase, m-galactarate dehydratase, STM3697
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Engineering
Engineering on EC 4.2.1.42 - galactarate dehydratase
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Y90F
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is catalytically impaired. Structure of the mutant in complex with Mg2+ and galactarate has a well-defined C-terminal segment through residue 387, well-ordered electron density for galactarate, and Mg2+ ions in both metal sites for both protomers comprising the asymmetric unit
H328A
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
H328N
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
K197A
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
H328A
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inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
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H328N
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inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
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K197A
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inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
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K197A
inactive mutant enzyme, the structure of the K197A mutant enzyme complexed with Mg2+ and L-glucarate is determined by molecular replacement using the SeMet-substituted STM3697 structure as the search model