Information on EC 3.5.3.23 - N-succinylarginine dihydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.3.23
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RECOMMENDED NAME
GeneOntology No.
N-succinylarginine dihydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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-
L-arginine degradation II (AST pathway)
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-
Metabolic pathways
-
-
arginine metabolism
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SYSTEMATIC NAME
IUBMB Comments
N2-succinyl-L-arginine iminohydrolase (decarboxylating)
Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates [3]. This is the second 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).
CAS REGISTRY NUMBER
COMMENTARY hide
99676-41-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NCTC 10743
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-
Manually annotated by BRENDA team
strain NCTC 10743
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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
N2-succinyl-L-arginine + H2O
N2-succinyl-L-ornithine + NH3 + CO2
show the reaction diagram
additional information
?
-
-
no substrate: L-arginine, N2-acetylarginine, N2-glutamylarginine
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
N2-succinyl-L-arginine
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pH 7.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.065
-
mutant C365S, pH 7.5, 30°C
5.3
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wild-type, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48874
-
x * 48874, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48874, calculated
additional information
-
sequence-structure homology study
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme in complex with N2-succinyl-L-ornithine, mutant C365S in complex with N-succinyl-L-arginine
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C365S
-
about 1% of wild-type activity, crystallization data
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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immunization of mice with recombinant succinylarginine dihydrolase with a peptide sequence similar to an anti-prion epitope, induces anti-PrP auto-Abs with anti-prion activity and significantly retards survival times of the mice subsequently infected with Fukuoka-1 prions
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