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4.2.1.28: propanediol dehydratase

This is an abbreviated version!
For detailed information about propanediol dehydratase, go to the full flat file.

Word Map on EC 4.2.1.28

Reaction

Propane-1,2-diol
=
propanal
 +
H2O

Synonyms

1,2-propanediol dehydratase, 1,2-propanediol hydro-lyase, adenosylcobalamin-dependent diol dehydratase, AdoCbl-dependent diol dehydratase, cobalamin-dependent diol dehydratase, coenzyme B12-dependent diol dehydrase, coenzyme B12-dependent diol dehydratase, coenzyme-B12-dependent diol dehydratase, DDH, dehydratase, diol, dehydratase, propanediol, diol dehydrase, diol dehydratase, diol dehydratase alpha subunit, dioldehydrase, dioldehydratase, DL-1,2-propanediol hydro-lyase, DL-1,2-propanediol hydrolyase, GldCDE, meso-2,3-butanediol dehydrase, PduCDE, PduCDEGH, Propanediol dehydrase

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.28 propanediol dehydratase

Engineering

Engineering on EC 4.2.1.28 - propanediol dehydratase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D335A
D335N
-
inactive mutant
E170A
-
inactive mutant
E170A E170Q
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme
E170H
-
does not form (alpha-beta-gamma)complex
E170Q
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme
E221A
-
does not form (alpha-beta-gamma)complex
H143A
Halpha143A
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme
Halpha143E
-
site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes
Halpha143K
-
site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes
Halpha143L
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme
Halpha143Q
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme, irreversible inactivation by O2 in the absence of substrate at a much lower rate than the wild type, preference of the Halpha143Q mutant for (R)- and (S)-1,2-propanediols, kinetic parameters for each enantiomer, overview
Kbeta135A
-
site-directed mutagenesis, the mutant shows 42% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin
Kbeta135E
-
site-directed mutagenesis, the mutant shows 98% reduced activity compared to the wild-type enzyme
Kbeta135Q
-
site-directed mutagenesis, the mutant shows 27% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin
Kbeta135R
-
site-directed mutagenesis, the mutant shows 24% reduced activity compared to the wild-type enzyme
Q141A
-
partial activity
Q296A
-
increased Km for substrate(1,2-propanediol) by a factor of 250
Q336A
the mutant shows decreased activity (21%) compared to the wild type enzyme
S224A
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 5fold reduction in kcat/Km
S224C
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. About 100fold reduction in kcat/Km
S224N
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 100fold reduction in kcat/Km
S301A
the mutant shows decreased activity (76%) compared to the wild type enzyme
S301A/Q336A
the mutant shows lowest activity (9.8%) compared to the wild type enzyme
S362A
-
partial activity
Salpha224A
-
site-directed mutagenesis, the mutant shows 81% reduced activity compared to the wild-type enzyme, mechanism-based complete inactivation of the Salpha224A holoenzyme during catalysis by propan-1,2-diol leading to accumulation of cobalamin, mechanism, overview
Salpha224N
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
T172A
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 100fold reduction in kcat/Km
T172S
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 10fold reduction in kcat/Km
Q336A
-
the mutant shows decreased activity (21%) compared to the wild type enzyme
-
S301A
-
the mutant shows decreased activity (76%) compared to the wild type enzyme
-
S301A/Q336A
-
the mutant shows lowest activity (9.8%) compared to the wild type enzyme
-
additional information