Literature summary for 1.8.4.10 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.

Search for more literature for 1.8.4.10

Protein Variants

Protein Variants	Comment	Organism
additional information	a heterologous system is constructed in which the C domain of EiAPR (EC 1.8.4.9) is fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (EC 1.8.4.10), 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 APS reduction. The ability to use glutathione is enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR	Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0114	-	5'-adenylyl sulfate	-	Pseudomonas aeruginosa
0.054	-	thioredoxin	-	Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe-S cluster	[4Fe-4S] cluster	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'-adenylyl sulfate + thioredoxin	-	Pseudomonas aeruginosa	AMP + sulfite + thioredoxin disulfide	-	?

Synonyms

Synonyms	Comment	Organism
PaAPR	-	Pseudomonas aeruginosa

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)