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Information on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming) and Organism(s) Alcanivorax borkumensis and UniProt Accession Q0VPF7

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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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This record set is specific for:
Alcanivorax borkumensis
UNIPROT: Q0VPF7 not found.
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Word Map
The taxonomic range for the selected organisms is: Alcanivorax borkumensis
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
succinate coenzyme A ligase
-
succinate-CoA ligase
-
A-SCS
-
-
-
-
A-STK
-
-
-
-
SCS-alpha
-
-
-
-
SCS-beta
-
-
-
-
SCS-betaA
-
-
-
-
STK
-
-
-
-
succinate coenzyme A ligase
-
Succinate thiokinase
-
-
-
-
succinate-CoA ligase
-
Succinic thiokinase
-
-
-
-
Succinyl coenzyme A synthetase
-
-
-
-
Succinyl coenzyme A synthetase (adenosine diphosphate-forming)
-
-
-
-
Succinyl-CoA synthetase
-
-
-
-
Succinyl-CoA synthetase (ADP-forming)
-
-
-
-
Synthetase, succinyl coenzyme A (adenosine diphosphate-forming)
-
-
-
-
VEG239
-
-
-
-
VEG63
-
-
-
-
Vegetative protein 239
-
-
-
-
Vegetative protein 63
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9080-33-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
show the reaction diagram
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
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
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.241
ATP
recombinant enzyme, pH 7.4, 30°C
0.004
CoA
recombinant enzyme, pH 7.4, 30°C
4.243
D-malate
recombinant enzyme, pH 7.4, 30°C
1.509
Itaconate
recombinant enzyme, pH 7.4, 30°C
3.27
L-malate
recombinant enzyme, pH 7.4, 30°C
0.157
succinate
recombinant enzyme, pH 7.4, 30°C
0.241
ATP
recombinant enzyme, pH 7.4, 30°C
0.004
CoA
recombinant enzyme, pH 7.4, 30°C
4.243
D-malate
recombinant enzyme, pH 7.4, 30°C
1.509
Itaconate
recombinant enzyme, pH 7.4, 30°C
3.27
L-malate
recombinant enzyme, pH 7.4, 30°C
0.157
succinate
recombinant enzyme, pH 7.4, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
ATP
recombinant enzyme, pH 7.4, 30°C
1.6
CoA
recombinant enzyme, pH 7.4, 30°C
1.7
D-malate
recombinant enzyme, pH 7.4, 30°C
0.5
Itaconate
recombinant enzyme, pH 7.4, 30°C
1.1
L-malate
recombinant enzyme, pH 7.4, 30°C
2.7
succinate
recombinant enzyme, pH 7.4, 30°C
3.6
ATP
recombinant enzyme, pH 7.4, 30°C
1.6
CoA
recombinant enzyme, pH 7.4, 30°C
1.7
D-malate
recombinant enzyme, pH 7.4, 30°C
0.5
Itaconate
recombinant enzyme, pH 7.4, 30°C
1.1
L-malate
recombinant enzyme, pH 7.4, 30°C
2.7
succinate
recombinant enzyme, pH 7.4, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.8
ATP
recombinant enzyme, pH 7.4, 30°C
372.3
CoA
recombinant enzyme, pH 7.4, 30°C
0.4
D-malate
recombinant enzyme, pH 7.4, 30°C
3.1
Itaconate
recombinant enzyme, pH 7.4, 30°C
0.3
L-malate
recombinant enzyme, pH 7.4, 30°C
17.2
succinate
recombinant enzyme, pH 7.4, 30°C
14.8
ATP
recombinant enzyme, pH 7.4, 30°C
372.3
CoA
recombinant enzyme, pH 7.4, 30°C
0.4
D-malate
recombinant enzyme, pH 7.4, 30°C
3.1
Itaconate
recombinant enzyme, pH 7.4, 30°C
0.3
L-malate
recombinant enzyme, pH 7.4, 30°C
17.2
succinate
recombinant enzyme, pH 7.4, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.14
purified recombinant enzyme, pH 7.4, 30°C, succinyl-CoA/ADP formation
4.14
purified recombinant enzyme, pH 7.4, 30°C, succinyl-CoA/ADP formation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta-subunit; gene sucCD
UniProt
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography
recombinant C-terminally His-tagged enzyme 1.55fold from Escherichia coli strain BL21(DE3)-pLysS by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
gene sucCD, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)-pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nolte, J.C.; Schuermann, M.; Schepers, C.L.; Vogel, E.; Wuebbeler, J.H.; Steinbuechel, A.
Novel characteristics of succinate coenzyme A (succinate-CoA) ligases: conversion of malate to malyl-CoA and CoA-thioester formation of succinate analogues in vitro
Appl. Environ. Microbiol.
80
166-176
2014
Escherichia coli K-12 (P0A836), Escherichia coli K-12 (P0AGE9), Alcanivorax borkumensis (Q0VPF7), Alcanivorax borkumensis (Q0VPF8), Alcanivorax borkumensis, Advenella mimigardefordensis (W0PAN5), Advenella mimigardefordensis (W0PFR9), Advenella mimigardefordensis, Alcanivorax borkumensis SK2 (Q0VPF7), Alcanivorax borkumensis SK2 (Q0VPF8), Alcanivorax borkumensis SK2, Advenella mimigardefordensis DPN7 (W0PAN5), Advenella mimigardefordensis DPN7 (W0PFR9), Escherichia coli K-12 BL21 (P0A836), Escherichia coli K-12 BL21 (P0AGE9)
Manually annotated by BRENDA team