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Information on EC 6.2.1.13 - acetate-CoA ligase (ADP-forming) and Organism(s) Pyrococcus furiosus and UniProt Accession E7FHP1

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.13 acetate-CoA ligase (ADP-forming)
IUBMB Comments
Also acts on propanoate and, very slowly, on butanoate.
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: E7FHP1
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
acs iii, acetyl-coa synthetase (adp-forming), adp-acs, acetate:coa ligase [adp-forming], tk0944/tk0943 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetyl-CoA synthetase
-
-
Acetyl-CoA synthetase (ADP-forming)
-
-
-
-
acetyl-coenzyme A synthetase (ADP-forming)
Q9Y8L1
-
ACS
-
-
-
-
ADP-forming acetyl-CoA synthetase
-
-
PF1540
gene name alpha subunit
PF1787
gene name, beta-subunit
Synthetase, acetyl coenzyme A (adenosine diphosphate-forming)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetate:CoA ligase (ADP-forming)
Also acts on propanoate and, very slowly, on butanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
62009-85-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
-
r
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
-
92% of the activity relative to acetyl-CoA
-
?
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
show the reaction diagram
-
r, isoenzyme ACS II is active, ACS I not
-
-
?
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
-
r, isoenzyme ACS II is active, ACS I not
-
-
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
no activity with isoenzymes ACS I and ACS II
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
-
34% of the activity relative to acetate
-
-
?
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
show the reaction diagram
-
36% of the activity relative to acetate
-
-
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
show the reaction diagram
-
r, 250% of the activity relative to ADP
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
-
r
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no effect
additional information
-
contains neither iron nor other metals, such as copper, zinc, or magnesium
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
acetate
Q9Y8L0, Q9Y8L1
-
0.019
acetyl-CoA
Q9Y8L0, Q9Y8L1
-
0.06
ADP
Q9Y8L0, Q9Y8L1
-
0.09
ATP
Q9Y8L0, Q9Y8L1
-
0.021
CoA
Q9Y8L0, Q9Y8L1
-
0.1
phosphate
Q9Y8L0, Q9Y8L1
-
0.5 - 1.1
acetate
0.0039 - 0.082
acetyl-CoA
0.05 - 0.283
ADP
0.07 - 0.477
ATP
0.0139 - 0.0771
CoA
0.132 - 0.236
GDP
0.43
GTP
-
isoenzyme ACS I
0.457
Isobutyrate
-
isoenzyme ACS I
0.012 - 0.029
isobutyryl-CoA
0.004
phenylacetyl-CoA
-
isoenzyme ACS II
0.2 - 1.59
phosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
67
acetate
-
isoenzyme ACS II
42 - 157
acetyl-CoA
115 - 203
ADP
68 - 82
ATP
65 - 73
CoA
21 - 411
GDP
27
GTP
-
isoenzyme ACS II
66
indoleacetate
-
isoenzyme ACS II
22 - 55
Isobutyrate
8 - 121
isobutyryl-CoA
89
phenylacetate
-
isoenzyme ACS II
138
phenylacetyl-CoA
-
isoenzyme ACS II
117 - 182
phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
isoenzyme ACS II
64.6
-
isoenzyme ACS I
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
9
-
at 80°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
-
6: about 60% of maximal activity, 11: about 40% of maximal activity, isoenzyme ACS I
6 - 8
-
about 50% of maximal activity at pH 6 and 8
7 - 11
-
7: about 60% of maximal activity, 11: about 65% of maximal activity, isoenzyme ACS II
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
assay at
80
assay at, catalytic arsenolysis of acetyl-CoA
87
Q9Y8L0, Q9Y8L1
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
isoenzymes ACS I and ACS II are inactive at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Q9Y8L0, Q9Y8L1
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Q9Y8L0, Q9Y8L1
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
gel filtration
145000
150000
gel filtration
150000 - 165000
-
native PAGE
23000
-
2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
25000
25878
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
27000
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
45000
-
2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
47000
49965
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
His257alpha and His71beta are sites of transient phosphorylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, sitting-drop vapour-diffusion method, crystals belong to monoclinic space group C2, with unit-cell parameters a = 131.3, b = 186.1, c = 121.5, beta = 122.6°, and diffract at 2.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D212betaE
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced
E218alphaD
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced
E218alphaQ
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced
E218Dalpha
1-10% of wild-type activity
H257alphaD
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit
H257Dalpha
mutant shows no activity in either direction
H71betaA
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
half-life is 60 min, in presence of 1 M KCl no loss of activity after 2 h
110
-
half-life is 30 min
80
-
t1/2: 18 h for isoenzyme ACS I, 8 h for isoenzyme ACS II
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
salts stabilize against heat inactivation. In presence of 1 M KCl the enzyme does not lose activity after 2 h incubation
-
sensitivity towards heat inactivation is increased with storage at -20°C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to oxygen for 24 h
-
626
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1-2 mg/ml enzyme, in 20 mM Tris/HCl, pH 8.0, 2 mM MgCl2, 150 mM NaCl, stable for several weeks
-
on ice stable for 2 d
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
about 10fold, 15 min at 80ºC and subsequent anion-exchange chromatography
Q9Y8L0, Q9Y8L1
isoenzymes ACS I and ACS II
-
recombinant wild-type and mutant enzyme subunits from Escherichia coli strain BL21(DE3) by heat precipitation at 90°C for 30 min, followed by reconstitution of holoenzyme through hydrophobic interaction chromatography ultrafiltration, and gel filtration, the chromatographic steps are then repeated
wild-type end mutant enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
Q9Y8L0, Q9Y8L1
acdIa and acdIb genes encoding alpha- and beta-subunit of ACD, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed mixed and incubated on ice
Q9Y8L0, Q9Y8L1
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed, mixed and incubated on ice
Q9Y8L0, Q9Y8L1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schfer, T.; Schnheit, P.
Pyruvate metabolism of the hyperthermophilic archaebaterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalyzed by an acetyl-CoA synthetase (ADP forming)
Arch. Microbiol.
155
366-377
1991
Pyrococcus furiosus
-
Manually annotated by BRENDA team
Glasemacher, J.; Bock, A.K.; Schmid, R.; Schnheit, P.
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.
244
561-567
1997
Pyrococcus furiosus
Manually annotated by BRENDA team
Mai, X.; Adams, M.W.W.
Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
178
5897-5903
1996
Pyrococcus furiosus
Manually annotated by BRENDA team
Musfeldt, M.; Selig, M.; Schonheit, P.
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits
J. Bacteriol.
181
5885-5888
1999
Giardia intestinalis (Q9Y1N2), Pyrococcus furiosus (Q9Y8L0), Pyrococcus furiosus (Q9Y8L1)
Manually annotated by BRENDA team
Lehtioe, L.; Fabrichniy, I.; Hansen, T.; Schoenheit, P.; Goldman, A.
Unusual twinning in an acetyl coenzyme A synthetase (ADP-forming) from Pyrococcus furiosus
Acta Crystallogr. Sect. D
D61
350-354
2005
Pyrococcus furiosus
Manually annotated by BRENDA team
Braesen, C.; Schmidt, M.; Groetzinger, J.; Schoenheit, P.
Reaction mechanism and structural model of ADP-forming acetyl-CoA synthetase from the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a second active site histidine residue
J. Biol. Chem.
283
15409-15418
2008
Pyrococcus furiosus, Pyrococcus furiosus (E7FI45 and E7FHP1)
Manually annotated by BRENDA team
Schfer, T.; Schnheit, P.
Maltose fermentation to acetate, CO2 and H2 in the anaerobic hyperthermophilic archaeon Pyrococcus furiosus evidence for the operation of a novel sugar fermentation pathway
Arch. Microbiol.
158
188-202
1992
Pyrococcus furiosus
-
Manually annotated by BRENDA team