Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

galactarate
=
(2R,3S)-2,3-dihydroxy-5-oxohexanedioate
+
H2O

Synonyms

A9CG74, Dehydratase, galactarate, Galactarate dehydrase, galactarate dehydratase, galactarate dehydratase III, GalcD, GalrD, GalrD-III, L-talarate/galactarate dehydratase, m-galactarate dehydratase, STM3697

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.42 galactarate dehydratase

Engineering

Engineering on EC 4.2.1.42 - galactarate dehydratase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H45Q
-
has no detectable activity
R162N
-
retains a small amount of activity
Y164F
-
has no detectable activity
Y90F
-
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
-
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