Information on EC 2.3.1.109 - arginine N-succinyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.109
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RECOMMENDED NAME
GeneOntology No.
arginine N-succinyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + L-arginine = CoA + N2-succinyl-L-arginine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
L-arginine degradation II (AST pathway)
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Metabolic pathways
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arginine metabolism
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:L-arginine N2-succinyltransferase
Also acts on L-ornithine. This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [2,6].
CAS REGISTRY NUMBER
COMMENTARY hide
99676-48-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ADP1
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
NCTC 10743
-
-
Manually annotated by BRENDA team
IRC204
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-
Manually annotated by BRENDA team
IRC204
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-
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
succinyl-CoA + L-arginine
CoA + N2-succinyl-L-arginine
show the reaction diagram
succinyl-CoA + L-homoarginine
CoA + N2-succinyl-L-homoarginine
show the reaction diagram
-
-
-
-
?
succinyl-CoA + L-ornithine
CoA + N2-succinyl-L-ornithine
show the reaction diagram
additional information
?
-
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 + L-arginine
CoA + N2-succinyl-L-arginine
show the reaction diagram
succinyl-CoA + L-ornithine
CoA + N2-succinyl-L-ornithine
show the reaction diagram
-
ornithine catabolic pathway
-
-
?
additional information
?
-
-
inactivation of the gene for arginine succinyltransferase (astA) resulted in a 7-fold increase in cyanophycin content
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
succinyl-CoA
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-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arginine
-
competitive inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
-
allosteric activator of the ornithine succinyltransferase activity
L-lysine
-
activator of the ornithine succinyltransferase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 5
L-arginine
0.04
L-ornithine
-
-
0.04
succinyl-CoA
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
agmatine
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-
2.6
D-arginine
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-
0.9
spermidine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007 - 0.37
-
depending on growth substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
L-homoarginine as substrate
8.7
-
L-arginine as substrate
9
-
L-ornithine as substrate
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
2 * 35000 + 2 * 37000, heterotetramer, SDS-PAGE
37000
-
2 * 35000 + 2 * 37000, heterotetramer, SDS-PAGE
150000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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2 * 35000 + 2 * 37000, heterotetramer, SDS-PAGE
additional information
-
three-dimensional structure analysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, retains full activity with both substrates for several weeks, loses 10-40% of its activity following repeated freezing and thawing
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4°C, 10 mM potassium phosphate, pH 7.5, stable for 48 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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