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Information on EC 3.5.3.23 - N-succinylarginine dihydrolase and Organism(s) Escherichia coli and UniProt Accession P76216

for references in articles please use BRENDA:EC3.5.3.23
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EC Tree
IUBMB Comments
Arginine, N2-acetylarginine and N2-glutamylarginine do not act as substrates . This is the second enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine . 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).
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This record set is specific for:
Escherichia coli
UNIPROT: P76216
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-succinylarginine dihydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 SOURCE
PATHWAYS
-
-
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
-
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
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.065
mutant C365S, pH 7.5, 30°C
5.3
wild-type, pH 7.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C365S
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, B.L.; Kiupakis, A.K.; Reitzer, L.J.
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli
J. Bacteriol.
180
4278-4286
1998
Escherichia coli
Manually annotated by BRENDA team
Shirai, H.; Mizuguchi, K.
Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism
FEBS Lett.
555
505-510
2003
Escherichia coli (P76216)
Manually annotated by BRENDA team
Tocilj, A.; Schrag, J.D.; Li, Y.; Schneider, B.L.; Reitzer, L.; Matte, A.; Cygler, M.
Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli
J. Biol. Chem.
280
15800-15808
2005
Escherichia coli (P76216), Escherichia coli
Manually annotated by BRENDA team
Ishibashi, D.; Yamanaka, H.; Mori, T.; Yamaguchi, N.; Yamaguchi, Y.; Nishida, N.; Sakaguchi, S.
Antigenic mimicry-mediated anti-prion effects induced by bacterial enzyme succinylarginine dihydrolase in mice
Vaccine
29
9321-9328
2011
Escherichia coli
Manually annotated by BRENDA team