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Information on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming) and Organism(s) Advenella mimigardefordensis and UniProt Accession W0PAN5
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6.2.1.5 succinate-CoA ligase (ADP-forming)Specify your search results
Word Map
- 6.2.1.5
- mtdna
- suclg1
-
methylmalonic
-
aciduria
- dguok
-
encephalomyopathic
- c10orf2
- mimigardefordensis
- twinkle
-
c4-dicarboxylic
- thiokinase
-
faroe
-
gtp-forming
-
hepatocerebral
-
3,3'-dithiodipropionic
- molecular biology
The taxonomic range for the selected organisms is: Advenella mimigardefordensis
The enzyme appears in selected viruses and cellular organisms
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, succinate coenzyme a ligase, succinyl-coa synthetase subunit alpha, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-SCS
-
-
-
-
A-STK
-
-
-
-
SCS-alpha
-
-
-
-
SCS-beta
-
-
-
-
SCS-betaA
-
-
-
-
STK
-
-
-
-
Succinate thiokinase
-
-
-
-
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
-
-
-
-
Succinyl coenzyme A synthetase
-
-
-
-
Succinyl-CoA synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
succinate:CoA ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9080-33-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + D-malate + CoA
ADP + phosphate + D-malyl-CoA
-
-
-
r
ATP + L-malate + CoA
ADP + phosphate + L-malyl-CoA
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
-
-
-
r
ATP + 3-sulfinopropionate + CoA
ADP + phosphate + 3-sulfinopropionyl-CoA
SucCDAm is unspecific regarding ATP or GTP
determination of 3-sulfinopropionyl-CoA structure by using liquid chromatography-electrospray ionization-mass spectrometry
-
?
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
succinate is the best substrate, SucCDAm is unspecific regarding ATP or GTP
-
-
?
additional information
?
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
additional information
?
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
additional information
?
-
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
additional information
?
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
additional information
?
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
additional information
?
-
-
substrate specificity, overview. Besides the preference for the physiological substrates succinate, itaconate, ATP, and CoA, high enzyme activity is additionally determined for both enantiomeric forms of malate, amounting to 10-21% of the activity with succinate, strong resemblance of SucCD to L-malate-CoA ligase, EC 6.2.1.9. No activity with sulfosuccinate, mercaptosuccinate, tartrate, acetate, butyrate, propionate, levulinate, valerate, malonate, glutarate, adipate, 3-sulfinopropionate, fumarate, maleate, and 2,2'-thiodiacetate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + itaconate + CoA
ADP + phosphate + itaconyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
SucCDAm is unspecific regarding ATP or GTP
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.964
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
2.964
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
0.2
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
1
3-sulfinopropionate
recombinant enzyme, pH 7.4, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
purified recombinant enzyme, pH 7.4, 30°C, succinyl-CoA/ADP formation
1 - 2
purified recombinant enzyme, pH 7.4, 30°C, succinyl-CoA/ADP formation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
transposon mutagenesis and deletion of gene sucCD, accumulation of 3SP during 3,3'-dithiodipropionic acid degradation occurs in Tn5::mob-induced mutants of Advenella mimigardefordensis strain DPN7T disrupted in sucCD and in the defined deletion mutant Advenella mimigardefordensis DELTAsucCD
additional information
transposon mutagenesis and deletion of gene sucCD, accumulation of 3SP during 3,3'-dithiodipropionic acid degradation occurs in Tn5::mob-induced mutants of Advenella mimigardefordensis strain DPN7T disrupted in sucCD and in the defined deletion mutant Advenella mimigardefordensis DELTAsucCD
additional information
-
transposon mutagenesis and deletion of gene sucCD, accumulation of 3SP during 3,3'-dithiodipropionic acid degradation occurs in Tn5::mob-induced mutants of Advenella mimigardefordensis strain DPN7T disrupted in sucCD and in the defined deletion mutant Advenella mimigardefordensis DELTAsucCD
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography
recombinant enzyme 1.07fold from Escherichia coli strain BL21(DE3)-pLysS by two different steps of anion exchange chromatography and affinity chromatography
recombinant soluble enzyme from Escherichia coli strain BL21(DE3)/pLysS by anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS
gene sucCD, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pLysS
gene sucCD, expression in Escherichia coli strain BL21(DE3)-pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuermann, M.; Wuebbeler, J.H.; Grote, J.; Steinbuechel, A.
Novel reaction of succinyl coenzyme A (succinyl-CoA) synthetase: activation of 3-sulfinopropionate to 3-Sulfinopropionyl-CoA in Advenella mimigardefordensis strain DPN7T during degradation of 3,3-dithiodipropionic acid
J. Bacteriol.
193
3078-3089
2011
Advenella mimigardefordensis (B3TZD8), Advenella mimigardefordensis (B3TZD9), Advenella mimigardefordensis, Advenella mimigardefordensis DPN7T (B3TZD8), Advenella mimigardefordensis DPN7T (B3TZD9)
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)
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