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ATP + 3-hydroxybutyrate + CoA
AMP + diphosphate + 3-hydroxybutyryl-CoA
ATP + 3-hydroxypropionate + CoA
AMP + diphosphate + 3-hydroxypropionyl-CoA
9% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
ATP + 3-hydroxybutyrate + CoA
AMP + diphosphate + 3-hydroxybutyryl-CoA
8% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + 3-hydroxybutyrate + CoA
AMP + diphosphate + 3-hydroxybutyryl-CoA
8% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
-
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme has a clear preference for unsubstituted straight chain organic acids with a chain length of four or five carbons. No activity is detected with the six-carbon hexanoic acid
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
tzhe enzyme is also a promiscuous acetate/propionate ligase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
wild-type enzyme shows no activity, mutant enzyme W424G shows activity
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme has a clear preference for unsubstituted straight chain organic acids with a chain length of four or five carbons. No activity is detected with the six-carbon hexanoic acid
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
tzhe enzyme is also a promiscuous acetate/propionate ligase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
-
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
wild-type enzyme shows no activity, mutant enzyme W424G shows activity
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
-
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
-
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
13% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
13% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
22% of the activity compared to 4-hydroxybutanoate
-
-
?
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
22% of the activity compared to 4-hydroxybutanoate
-
-
?
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ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
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physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is involved in autotrophic CO2 fixation
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle
-
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway. The flux between the succinate and acetyl-CoA branches in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway is governed by 4-hydroxybutyrate-CoA ligase, possibly regulated posttranslationally by the protein acetyltransferase
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation
-
physiological function
-
the enzyme is involved in autotrophic carbon fixation
-
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Hawkins, A.S.; Han, Y.; Bennett, R.K.; Adams, M.W.; Kelly, R.M.
Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in thermoacidophilic archaea
J. Biol. Chem.
288
4012-4022
2013
Metallosphaera sedula (A4YDR9), Metallosphaera sedula (A4YDT1), Metallosphaera sedula (A4YGF9), Metallosphaera sedula, Metallosphaera sedula DSM 5348 (A4YDR9), Metallosphaera sedula DSM 5348 (A4YDT1), Metallosphaera sedula DSM 5348 (A4YGF9)
brenda
Hawkins, A.B.; Adams, M.W.; Kelly, R.M.
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
Appl. Environ. Microbiol.
80
2536-2545
2014
Metallosphaera sedula (A4YDT1), Metallosphaera sedula, Metallosphaera sedula DSM 5348 (A4YDT1)
brenda
Ramos-Vera, W.H.; Labonte, V.; Weiss, M.; Pauly, J.; Fuchs, G.
Regulation of autotrophic CO2 fixation in the archaeon Thermoproteus neutrophilus
J. Bacteriol.
192
5329-5340
2010
Pyrobaculum neutrophilum (B1YBY4), Pyrobaculum neutrophilum DSM 2338 (B1YBY4)
brenda
Ramos-Vera, W.H.; Weiss, M.; Strittmatter, E.; Kockelkorn, D.; Fuchs, G.
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota
J. Bacteriol.
193
1201-1211
2011
Pyrobaculum neutrophilum (B1YBY4), Pyrobaculum neutrophilum DSM 2338 (B1YBY4)
brenda