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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

Cloned

Cloned on EC 4.2.1.28 - propanediol dehydratase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-subunit DNA and amino acid sequence determination and analysis, sequence comparison, and expression of wild-type and chimeric mutants, in Escherichia coli strain BL21(DE3), distribution of the chimeric mutants in recombinant bacterial cells, overview
catabolite-responsive element sequence immediately upstream of the pdu operon encoding diol dehydratase and metabolosome structural genes
-
expressed in Escherichia coli
-
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli Rosetta (DE3) cells
-
expression in E.coli
-
expression in Escherichia coli
expression in Escherichia coli of the three genes encoding the subunits of the enzyme. Recombinant protein cannot form an active complex
-
expression in Escherichia coli strain JM109
-
expression of fusion protein PduD1-18-eGFP from a plasmid in a pduCDE deletion mutant
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expression of wild-type and mutant enzymes in Escherichia coli
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gene pduC, DNA and amino acid sequence determination and analysis, genetic organization in the pdu operon, overview, and recombinant enzyme expression in Escherichia coli strain JM109
gene pduD, DNA and amino acid sequence determination and analysis, genetic organization in the pdu operon, overview, and recombinant enzyme expression in Escherichia coli strain JM109
gene pduE, DNA and amino acid sequence determination and analysis, genetic organization in the pdu operon, overview, and recombinant enzyme expression in Escherichia coli strain JM109
N-terminal truncations (20 or 16 amino acid residues) of either or both of the beta and gamma subunits are expressed on a high level in Escherichia coli. All the mutant enzymes obtained are expressed in a soluble, active form. The mutant enzyme with the N-terminal truncations of both beta and gamma subunits are indistinguishable in catalytic properties from recombinant wild-type enzyme of the enzyme purified from Klebsiella oxytoca in a soluble form
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overexpression in Escherichia coli strain JM109
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