Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.2.1.5 - succinate-CoA ligase (ADP-forming) and Organism(s) Mus musculus and UniProt Accession Q9Z2I9

for references in articles please use BRENDA:EC6.2.1.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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)
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q9Z2I9 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mus musculus
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 subunit alpha, succinyl-coa synthetase (adp-forming), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SCS A-beta
-
SCS ADP-forming beta subunit
-
succinyl-CoA synthase ADP-forming beta subunit
-
A-SCS
-
-
-
-
A-STK
-
-
-
-
ATP-forming SUCL
-
-
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)
-
-
-
-
SUCLA2
-
-
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
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-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
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
r
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit beta
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme deficiency induces severe mitochondrial dysfunction including lowered oxidative phosphorylation efficiency, increased mitochondrial superoxide production, and mitochondrial DNA depletion as well as aberrations of mitochondrial fusion and fission proteins, which eventually leads to neuronal stress
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUCB1_MOUSE
463
0
50114
Swiss-Prot
Mitochondrion (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kacso, G.; Ravasz, D.; Doczi, J.; Nemeth, B.; Madgar, O.; Saada, A.; Ilin, P.; Miller, C.; Ostergaard, E.; Iordanov, I.; Adams, D.; Vargedo, Z.; Araki, M.; Araki, K.; Nakahara, M.; Ito, H.; Gal, A.; Molnar, M.J.; Nagy, Z.; Patocs, A.; Adam-Vizi, V.; Chinopoulos, C.
Two transgenic mouse models for beta-subunit components of succinate-CoA ligase yielding pleiotropic metabolic alterations
Biochem. J.
473
3463-3485
2016
Mus musculus
Manually annotated by BRENDA team
Zhao, Y.; Tian, J.; Sui, S.; Yuan, X.; Chen, H.; Qu, C.; Du, Y.; Guo, L.; Du, H.
Loss of succinyl-CoA synthase ADP-forming ? subunit disrupts mtDNA stability and mitochondrial dynamics in neurons
Sci. Rep.
7
7169
2017
Mus musculus (Q9Z2I9)
Manually annotated by BRENDA team