Information on EC 6.2.1.B1 - O-succinylbenzoate-CoA ligase (ADP-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
O-succinylbenzoate-CoA ligase (ADP-forming)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-succinylbenzoate + CoA = ADP + phosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
O-succinylbenzoate:CoA ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
72506-70-8
identical to EC 6.2.1.26
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-succinylbenzoate + CoA
ADP + phosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
ATP + 2-succinylbenzoate + dephospho-CoA
ADP + phosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
-
26% of the activity with CoA
-
-
?
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
ATP + 2-succinylbenzoate + CoA
ADP + phosphate + 2-succinylbenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in anthraquinone biosynthesis
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-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
less efficient activation than Mg2+
Mg2+
-
activates
Mn2+
-
less efficient activation than Mg2+
Ni2+
-
less efficient activation than Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0881
ATP
-
-
0.0599
CoA
-
-
0.1158
o-succinylbenzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000834
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
phosphoralyted enzyme form, isoelectric focusing
8.7
-
non-phosphorylated enzyme form, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
enzyme in crude extract, half-life: 9.3 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25°C, enzyme in crude extract has a half-life of 672 h
-
4°C, enzyme in crude extract has a half-life of 37 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE