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Literature summary for 3.5.1.78 extracted from

  • Pai, C.H.; Wu, H.J.; Lin, C.H.; Wang, A.H.
    Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases (2011), Protein Sci., 20, 557-566.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzyme C59A is expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme C59A in complex with glutathionylspermidine Escherichia coli

Protein Variants

Protein Variants Comment Organism
C59A active site mutant Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glutathionylspermidine + H2O Escherichia coli
-
glutathione + spermidine
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AES0 bifunctional enzyme glutathionylspermidine synthetase/amidase
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathionylspermidine + H2O
-
Escherichia coli glutathione + spermidine
-
?

Synonyms

Synonyms Comment Organism
Glutathionylspermidine synthetase/amidase bifunctional enzyme Escherichia coli
GSP amidase
-
Escherichia coli
GspA glutathionylspermidine amidase domain of GspSA Escherichia coli
GspSA bifunctional enzyme Escherichia coli