MetaCyc Enzyme: acetate-CoA ligase (ADP-forming)

Synonyms: acetyl-CoA synthetase (ADP-forming), ADP-dependent acetyl coenzyme A synthetase

Species: Pyrococcus furiosus

Subunit composition of acetate-CoA ligase (ADP-forming) = [AcdA]2[AcdB]2
         acetate-CoA ligase α subunit = AcdA (summary available)
         acetate-CoA ligase β subunit = AcdB (summary available)

This enzyme couples acetate formation from acetyl-CoA with phosphorylation of ADP using a substrate-level phosphorylation mechanism. In Pyrococcus furiosus, this enzyme is the ATP conserving step of pyruvate, or sugar fermentation to acetate. Two isoforms of this enzyme exist in this organism. Isoform I, the enzyme shown here, preferentially uses acetyl-CoA as a substrate and appears to be the physiologically relevant enzyme in this glycolysis and fermentation pathway. The other isoform, II, has been implicated in fermentation of aromatic amino acids (reviewed in [Sakuraba02]).

Molecular Weight: 140 kD (experimental) [Hutchins01]

Gene-Reaction Schematic

Gene-Reaction Schematic

Enzymatic reaction of: acetate-CoA ligase (ADP-forming)

Inferred from experiment

EC Number:

acetate + ATP + coenzyme A ⇄ acetyl-CoA + ADP + phosphate

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

This reaction is reversible.

Alternative Substrates for acetate: isobutanoate [Hutchins01]
Alternative Substrates for ADP: GDP [Hutchins01]

In Pathways: pyruvate fermentation to acetate and alanine, pyruvate fermentation to acetate III, acetate formation from acetyl-CoA II

This enzyme catalyzes the reversible conversion of acetyl-CoA, ADP and phosphate to acetate, ATP and CoA [Glasemacher97]. The pH optimum of 9.0 was determined at 80 deg. C [Mai96a].

Kinetic Parameters:
Substrate Km (μM) Citations
phosphate 396.0 [Hutchins01]
acetyl-CoA 25.0 [Hutchins01]
ADP 150.0 [Hutchins01]

T(opt): 90 °C [Glasemacher97]

pH(opt): 9.0 [Mai96a]

Subunit of acetate-CoA ligase (ADP-forming): acetate-CoA ligase α subunit

Synonyms: AcdA

Gene: acdA Accession Number: G-9185 (MetaCyc)

Molecular Weight: 49.965 kD (from nucleotide sequence)

Molecular Weight: 45 kD (experimental) [Hutchins01]

Unification Links: ModBase:Q9Y8L1, Pride:E7FI45, Protein Model Portal:E7FI45, Swiss-Model:Q9Y8L1, UniProt:Q9Y8L1

Relationship Links: InterPro:IN-FAMILY:IPR003781, InterPro:IN-FAMILY:IPR014089, InterPro:IN-FAMILY:IPR016040, InterPro:IN-FAMILY:IPR016102, Pfam:IN-FAMILY:PF13380, Smart:IN-FAMILY:SM00881

The subunit molecular mass was determined by SDS-PAGE [Hutchins01].

Subunit of acetate-CoA ligase (ADP-forming): acetate-CoA ligase β subunit

Synonyms: AcdB

Gene: acdB Accession Number: G-9186 (MetaCyc)

Molecular Weight: 25.878 kD (from nucleotide sequence)

Molecular Weight: 23 kD (experimental) [Hutchins01]

Unification Links: ModBase:Q9Y8L0, Pride:E7FHP1, Protein Model Portal:E7FHP1, SMR:E7FHP1, Swiss-Model:Q9Y8L0, UniProt:Q9Y8L0

Relationship Links: InterPro:IN-FAMILY:IPR011761, InterPro:IN-FAMILY:IPR013816, Pfam:IN-FAMILY:PF08442, Prosite:IN-FAMILY:PS50975

The subunit molecular mass was determined by SDS-PAGE [Hutchins01].


Glasemacher97: Glasemacher J, Bock AK, Schmid R, Schonheit P (1997). "Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus." Eur J Biochem 1997;244(2);561-7. PMID: 9119024

Hutchins01: Hutchins AM, Mai X, Adams MW (2001). "Acetyl-CoA synthetases I and II from Pyrococcus furiosus." Methods Enzymol 331;158-67. PMID: 11265458

Mai96a: Mai X, Adams MW (1996). "Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus." J Bacteriol 1996;178(20);5897-903. PMID: 8830684

Sakuraba02: Sakuraba H, Ohshima T (2002). "Novel energy metabolism in anaerobic hyperthermophilic archaea: a modified Embden-Meyerhof pathway." J Biosci Bioeng 93(5);441-8. PMID: 16233230

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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