Information on EC 3.1.2.3 - succinyl-CoA hydrolase

for references in articles please use BRENDA:EC3.1.2.3
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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
3.1.2.3
-
top print hide
RECOMMENDED NAME
GeneOntology No.
succinyl-CoA hydrolase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + H2O = CoA + succinate
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
-
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA hydrolase
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9025-86-9
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutaryl-CoA + H2O
CoA + glutarate
show the reaction diagram
-
-
-
-
?
succinyl CoA + H2O
CoA + succinate
show the reaction diagram
succinyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme is responsible for the termination of beta-oxidation of dicarboxylic acids of medium chain length
-
-
-
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
enzyme is responsible for the termination of beta-oxidation of dicarboxylic acids of medium chain length
-
-
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37.1
glutaryl-CoA
-
-
13.3
succinyl-CoA
-
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.14
-
substrate glutaryl-CoA
3.98
-
substrate succinyl-CoA
additional information
-
change of optical density per min
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
ultracentrifugation
top print hide
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sequence contains a putative consensus type 1 peroxisome targeting signal
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, stable for months
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
-
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.2.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)