Literature summary for 1.8.4.9 extracted from

Kim, S.K.; Gomes, V.; Gao, Y.; Chandramouli, K.; Johnson, M.K.; Knaff, D.B.; Leustek, T.
The two-domain structure of 5-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity (2007), Biochemistry, 46, 591-601.

Cloned(Commentary)

Cloned (Comment)	Organism
a heterologous system is constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR can use both thioredoxin and glutathione as an electron donor for 5'-adenylylsulfate reduction. Expression in Escherichia coli	Ulva intestinalis

Cloned (Comment)

Organism

a heterologous system is constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR can use both thioredoxin and glutathione as an electron donor for 5'-adenylylsulfate reduction. Expression in Escherichia coli

Ulva intestinalis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0002	-	glutathione	-	Ulva intestinalis
0.011	-	5'-adenylyl sulfate	-	Ulva intestinalis

Organism

Organism	UniProt	Comment	Textmining
Ulva intestinalis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Ulva intestinalis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'-adenylyl sulfate + glutathione	-	Ulva intestinalis	AMP + sulfite + glutathione disulfide	-	?

Synonyms

Synonyms	Comment	Organism
EiAPR	-	Ulva intestinalis

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Release 2023.1 (January 2023)