4.2.1.120: 4-hydroxybutanoyl-CoA dehydratase
This is an abbreviated version!
For detailed information about 4-hydroxybutanoyl-CoA dehydratase, go to the full flat file.
Word Map on EC 4.2.1.120
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4.2.1.120
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crotonyl-coa
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aminobutyricum
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4-hydroxybutyrate
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succinyl-coa
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3-hydroxypropionate/4-hydroxybutyrate
-
2-hydroxyacyl-coa
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sedula
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metallosphaera
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chemolithoautotrophic
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non-redox
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thermoproteales
-
ignicoccus
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autotrophy
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thermoproteus
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kluyveri
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hospitalis
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neutrophilus
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sulfolobales
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dicarboxylate/4-hydroxybutyrate
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hexacyanoferrateiii
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ketyl
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crenarchaeota
- 4.2.1.120
- crotonyl-coa
- aminobutyricum
- 4-hydroxybutyrate
- succinyl-coa
-
3-hydroxypropionate/4-hydroxybutyrate
-
2-hydroxyacyl-coa
- sedula
- metallosphaera
-
chemolithoautotrophic
-
non-redox
- thermoproteales
-
ignicoccus
-
autotrophy
-
thermoproteus
- kluyveri
- hospitalis
- neutrophilus
- sulfolobales
-
dicarboxylate/4-hydroxybutyrate
-
hexacyanoferrateiii
-
ketyl
- crenarchaeota
Reaction
Synonyms
4-hydroxybutyryl-CoA dehydratase, 4-hydroxybutyryl-coenzyme A dehydratase, 4HBD, AbfD, Igni_0595, Msed_1321, Tneu_0422
ECTree
4.2.1.120 4-hydroxybutanoyl-CoA dehydrataseAdvanced search results
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results (Engineering
Engineering on EC 4.2.1.120 - 4-hydroxybutanoyl-CoA dehydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A460G
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
C103A
site-directed mutagenesis of a catalytic residue, inactive mutant with monomeric, dimeric, or tetrameric subunit composition compared to wild-type
C299A
site-directed mutagenesis of a catalytic residue, inactive mutant with monomeric, dimeric, or tetrameric subunit composition compared to wild-type
C99A
site-directed mutagenesis of a catalytic residue, inactive mutant with monomeric, dimeric, or tetrameric subunit composition compared to wild-type
E257Q
site-directed mutagenesis, inactive mutant forming tetramers
E455Q
site-directed mutagenesis, inactive mutant forming tetramers
H292C
site-directed mutagenesis of a catalytic residue, inactive mutant with dimeric or tetrameric subunit composition compared to wild-type
H292E
site-directed mutagenesis of a catalytic residue, inactive mutant with tetrameric subunit composition compared to wild-type
K300Q
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
M149S
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
Q101E
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
R90N
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
T190V
Y296F
site-directed mutagenesis, almost inactive mutant forming tetramers
additional information
iron and FAD contents of enzyme mutants compared to the wild-type, mutant phenotypes, overview
T190V
site-directed mutagenesis, almost inactive mutant forming tetramers
T190V
site-directed mutagenesis, the mutant shows highly reduced enzyme activity and forms tetramers
