Information on EC 3.5.3.23 - N-succinylarginine dihydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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
L-arginine degradation II (AST pathway)
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arginine metabolism
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Arginine and proline metabolism
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Metabolic pathways
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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
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
?
-
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no substrate: L-arginine, N2-acetylarginine, N2-glutamylarginine
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-
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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
UNIPROT
ORGANISM
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
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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
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about 1% of wild-type activity, crystallization data
additional information
-
disruption of astB eliminates succinylarginine dihydrolase activity and prevents arginine utilization but does not impair ornithine catabolism
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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