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Information on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming) and Organism(s) Acetobacter aceti and UniProt Accession B3EY95

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.5 succinate-CoA ligase (ADP-forming)
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Select one or more organisms in this record: ?
This record set is specific for:
Acetobacter aceti
UNIPROT: B3EY95 not found.
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Word Map
The taxonomic range for the selected organisms is: Acetobacter aceti
The enzyme appears in selected viruses and cellular organisms
Synonyms
sucla2, succd, a-scs, cg11963, scact, adp-forming succinyl-coa synthetase, scs-betaa, a-stk, succinyl-coa synthetase (adp-forming), succinyl-coa ligase (atp-forming), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
succinyl-CoA:acetate CoA-transferase
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succinyl-coenzyme A:acetate CoA-transferase
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A-SCS
-
-
-
-
A-STK
-
-
-
-
SCS-alpha
-
-
-
-
SCS-beta
-
-
-
-
SCS-betaA
-
-
-
-
STK
-
-
-
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Succinate thiokinase
-
-
-
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Succinic thiokinase
-
-
-
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Succinyl coenzyme A synthetase
-
-
-
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Succinyl coenzyme A synthetase (adenosine diphosphate-forming)
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-
-
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Succinyl-CoA synthetase
-
-
-
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Succinyl-CoA synthetase (ADP-forming)
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-
-
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Synthetase, succinyl coenzyme A (adenosine diphosphate-forming)
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-
-
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VEG239
-
-
-
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VEG63
-
-
-
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Vegetative protein 239
-
-
-
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Vegetative protein 63
-
-
-
-
additional information
AarC is predicted to be a class I CoAtransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
show the reaction diagram
reaction mechanism, Glu435 is a key active site residue, overview. Class I CoA-transferases first bind the acyl-CoA substrate, forming a carboxylate product and an enzyme-CoA thioester intermediate, which accounts for the observed ping-pong kinetics and susceptibility to borohydride inactivation
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9080-33-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
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
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
AarC is succinyl-CoA:acetate CoA-transferase, which replaces succinyl-CoA synthetase in a variant CAC, this new bypass appears to reduce metabolic demand for free CoA, reliance upon nucleotide pools, and the likely effect of variable cytoplasmic pH upon CAC flux, the enzyme is required for the citric acid cycle, overview
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Borohydride
inactivation, in the presence of acetyl-CoA causes near-complete loss of enzyme activity consistent with the reduction of the glutamyl-CoA thioester intermediate to 5-hydroxynorvaline, in absence of acetyl-CoA only partial inactivation, 71% activity relative to a control, occurs
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70
acetate
pH 8.0, 25°C
0.0223
acetyl-CoA
pH 8.0, 25°C
0.9
succinate
pH 8.0, 25°C
0.0221
succinyl-CoA
pH 8.0, 25°C
additional information
additional information
kinetic analysis, parameters at different conditions, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
280
acetate
pH 8.0, 25°C
75.2
acetyl-CoA
pH 8.0, 25°C
70.9
succinate
pH 8.0, 25°C
201
succinyl-CoA
pH 8.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.053
strain 2002, reverse reaction
0.083
strain 1023, reverse reaction
0.114
strain 2002, forward reaction
0.17
strain 1023, forward reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains 1023 and DSM 2002, aarABC region, gene aarC
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SCACT_ACEAC
505
0
54826
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55832
x * 55846, recombinant enzyme, x * 55832, recombinant, borohydride-treated enzyme
55846
x * 55846, recombinant enzyme, x * 55832, recombinant, borohydride-treated enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55846, recombinant enzyme, x * 55832, recombinant, borohydride-treated enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by ammonium sulfate fractionation and metal affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aarC, DNA and amino acid sequence determination and analysis, expression analysis, overexpression as soluble His6-tagged enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mullins, E.A.; Francois, J.A.; Kappock, T.J.
A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti
J. Bacteriol.
190
4933-4940
2008
Acetobacter aceti (B3EY95)
Manually annotated by BRENDA team