Literature summary for 3.5.1.78 extracted from

Oza, S.L.; Ariyanayagam, M.R.; Fairlamb, A.H.
Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata (2002), Biochem. J., 364, 679-686.

Search for more literature for 3.5.1.78

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli, His6-tag	Crithidia fasciculata

Protein Variants

Protein Variants	Comment	Organism
C79A	complete loss of amidase activity without affecting synthetase activity	Crithidia fasciculata

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.059	-	spermidine	pH 7.3, synthetase activity	Crithidia fasciculata
0.114	-	ATP	pH 7.3, synthetase activity	Crithidia fasciculata
0.242	-	reduced glutathione	pH 7.3, synthetase activity	Crithidia fasciculata
0.5	-	glutathionylspermidine	pH 7.3, amidase activity	Crithidia fasciculata

Organism

Organism	UniProt	Comment	Textmining
Crithidia fasciculata	-	bifunctional glutathionylspermidine synthetase, EC 6.3.1.8, and amidase, EC 3.5.1.78	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Crithidia fasciculata

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
glutathionylspermidine + H2O	-	Crithidia fasciculata	glutathione + spermidine	-	r
trypanothione + H2O	hydrolysis at 1.5% the rate of glutathionylspermidine	Crithidia fasciculata	glutathione + glutathionylspermidine	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)