Literature summary for 6.3.1.8 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant C59A lacking amidase activity, in complex with amidase substrate gluthionylspermidine and ADP. Homodimer, and each monomer contains the N-terminal amidase and C-terminal synthetase domains connected by a linker in between	Escherichia coli

Organism

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

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Release 2023.1 (January 2023)