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Literature summary for 6.2.1.1 extracted from

  • Oberlies, G.; Fuchs, G.; Thauer, R.K.
    Acetate thiokinase and the assimilation of acetate in Methanobacterium thermoautotrophicum (1980), Arch. Microbiol., 128, 248-252.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
P1,P5-di(adenosine-5)pentaphosphate inhibits ADP formation Methanothermobacter thermautotrophicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
acetate
-
Methanothermobacter thermautotrophicus
0.05
-
CoA value above 0.05 mM Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Methanothermobacter thermautotrophicus acetate thiokinase is not involved in autotrophic CO2 fixation ?
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
specific activity of the enzyme is high in cells grown with limited H2 and CO2 supply. It is low in exponentially grown cells
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
Methanothermobacter thermautotrophicus AMP + diphosphate + acetyl-CoA
-
?
additional information acetate thiokinase is not involved in autotrophic CO2 fixation Methanothermobacter thermautotrophicus ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
Methanothermobacter thermautotrophicus