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
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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
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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
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Cofactor
Cofactor on EC 4.2.1.120 - 4-hydroxybutanoyl-CoA dehydratase
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[4Fe-4S]-center
the enzyme contains one [4Fe-4S]2x02 cluster per enzyme tetramer, reconstitution of the [4Fe-4S] cluster in the purified enzyme with FeCl3 and Na2S
4Fe-4S-center
a [4Fe-4S]2+ cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety
4Fe-4S-center
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enzyme shows [4Fe-4S]2+ clusters, two clusters/homotetramer. The four iron atoms in each cluster are coordinated in an identical fashion, and there is no direct interaction with substrates. The Fe-S clusters serve a structural rather than a catalytic role in 4-hydroxybutyryl-CoA dehydratase
4Fe-4S-center
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Fe-S-cluster is difficult to reduce. No equilibration of electrons between the flavin and the Fe-S-center
FAD
a [4Fe-4S]2+cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety
FAD
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protein-bound FAD, is easily reduced to the semiquinone and only slowly to the hydroquinone. No equilibration of electrons between the flavin and the Fe-S-center
FAD
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substrate interacts with the flavin. Partial reduction of the enzyme using dithionite results in formation of a neutral flavin semiquinone, which may interact with the 4Fe-4S-center
FAD
one FAD per enzyme subunit, FAD contents of enzyme mutants compared to the wild-type, overview