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Literature summary for 3.5.3.23 extracted from

  • 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 (2005), J. Biol. Chem., 280, 15800-15808.
    View publication on PubMed
Search for more literature for 3.5.3.23

Crystallization (Commentary)

Crystallization (Comment) Organism
native enzyme in complex with N2-succinyl-L-ornithine, mutant C365S in complex with N-succinyl-L-arginine Escherichia coli

Protein Variants

Protein Variants Comment Organism
C365S about 1% of wild-type activity, crystallization data Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P76216
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
N2-succinyl-L-arginine + 2 H2O = N2-succinyl-L-ornithine + 2 NH3 + CO2 mechanism consists of two cycles of hydrolysis and ammonia release, with each cycle utilizing a mechanism similar to that proposed for arginine deiminases Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.065
-
 mutant C365S, pH 7.5, 30°C Escherichia coli
5.3
-
 wild-type, pH 7.5, 30°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N2-succinyl-L-arginine + H2O
-
 Escherichia coli N2-succinyl-L-ornithine + NH3 + CO2
-
 ?

Synonyms

Synonyms Comment Organism
AstB
-
 Escherichia coli