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Literature summary for 1.8.4.8 extracted from

  • Chung, J.S.; Noguera-Mazon, V.; Lancelin, J.M.; Kim, S.K.; Hirasawa, M.; Hologne, M.; Leustek, T.; Knaff, D.B.
    Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase (2009), J. Biol. Chem., 284, 31181-31189.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.8

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 thioredoxin I wild type enzyme, at 20°C in 10 mM phosphate buffer (pH 7.5) containing 100 mM Na2SO4 Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine 5'-phosphosulfate + thioredoxin I
-
 Pseudomonas aeruginosa AMP + sulfite + oxidized thioredoxin I
-
 ?
additional information thioredoxin I mutant W31A shows no detectable activity, whereas W31F, K36E, and D61N are able to serve as electron donors for the APR-catalyzed reaction but with lower turnover numbers than that exhibited by the wild type thioredoxin I. The Km for thioredoxin mutant R73E is increased by 7.7fold compared with wild type thioredoxin I Pseudomonas aeruginosa ?
-
 ?

Synonyms

Synonyms Comment Organism
5'-adenylylsulfate reductase
-
 Pseudomonas aeruginosa
APR
-
 Pseudomonas aeruginosa
APS reductase
-
 Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
thioredoxin dependent on Pseudomonas aeruginosa