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Literature summary for 1.8.4.10 extracted from

  • Kopriva, S.; Fritzemeier, K.; Wiedemann, G.; Reski, R.
    The putative moss 3'-phosphoadenosine-5'-phosphosulfate reductase is a novel form of adenosine-5-phosphosulfate reductase without an iron-sulfur cluster (2007), J. Biol. Chem., 282, 22930-22938.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
(NH4)2SO4 activates Physcomitrium patens
KNO3 activates Physcomitrium patens
Mg2+ activates Physcomitrium patens
additional information PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein Physcomitrium patens
sulfate activates Physcomitrium patens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adenylyl sulfate + thioredoxin Physcomitrium patens sulfate assimilation pathway in Physcomitrella patens, overview AMP + sulfite + thioredoxin disulfide
-
?
additional information Physcomitrium patens the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes ?
-
?

Organism

Organism UniProt Comment Textmining
Physcomitrium patens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin the reaction catalyzed by APR can be divided into three steps. In the first step, APS binds to the protein, and a reductive transfer results in sulfite bound to the active-site cysteine in a stable reaction intermediate. In the second step, free sulfite is released by the action of free thioredoxin. In the third step, the thioredoxin is regenerated by reduction with thioredoxin reductase Physcomitrium patens

Storage Stability

Storage Stability Organism
-20┬░C, 1 day, PpAPR-B retains 30% of its activity Physcomitrium patens
4┬░C, PpAPR-B, completely stable for 5 days Physcomitrium patens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenylyl sulfate + thioredoxin sulfate assimilation pathway in Physcomitrella patens, overview Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?
adenylyl sulfate + thioredoxin dependent on thioredoxin, APS is the preferred substrate, substrate binding structure, modelling, overview Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?
additional information the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR, EC 1.8.4.8, genes Physcomitrium patens ?
-
?

Synonyms

Synonyms Comment Organism
APR
-
Physcomitrium patens
PpAPR-B
-
Physcomitrium patens

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
37
-
-
Physcomitrium patens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
PpAPR-B activity in terms of APS reduction increases gradually and less markedly with increasing pH compared to PpAPR, EC 1.8.4.9 Physcomitrium patens
8
-
-
Physcomitrium patens

Cofactor

Cofactor Comment Organism Structure
additional information PpAPR-B does not contain the FeS cluster, which is believed to determine the substrate specificity of other APR enzymes from seed plants. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein. No activity with glutathione or DTT Physcomitrium patens
thioredoxin
-
Physcomitrium patens