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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.9 expression of N-terminally His-tagged PpAPR in Escherichia coli, expression of GFP-tagged APR in Physcomitrella patens plants using the mAV4 vector containing the chloroplast transit peptide from Physcomitrella patens FtsZ2-1 and transient transfection of protoplasts Physcomitrium patens
1.8.4.9 overexpression in Escherichia coli Physcomitrium patens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.4.9 adenosine 5'-phosphosulfate inhibits activity with 3'-phosphoadenosine 5'-phosphosulfate Physcomitrium patens
1.8.4.9 glutathione inhibits APR at concentrations above 30 mM Physcomitrium patens
1.8.4.9 KNO3 abolishes enzyme activation by other salts and inhibits the enzyme Physcomitrium patens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.9 0.02
-
3'-phosphoadenosine 5'-phosphosulfate
-
Physcomitrium patens
1.8.4.9 0.05
-
adenosine 5'-phosphosulfate
-
Physcomitrium patens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.9 chloroplast
-
Physcomitrium patens 9507
-
1.8.4.9 chloroplast determination of subcellular localization, overview Physcomitrium patens 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.9 (NH4)2SO4 highly activating Physcomitrium patens
1.8.4.9 (NH4)2SO4 500 mM, stimulates Physcomitrium patens
1.8.4.9 Fe2+ FeS cluster as a cofactor in PpAPR Physcomitrium patens
1.8.4.9 KNO3 500 mM, stimulates Physcomitrium patens
1.8.4.9 Mg2+ activates 18-24fold at 500 mM Physcomitrium patens
1.8.4.9 MgCl2 500 mM, stimulates Physcomitrium patens
1.8.4.9 MgSO4 500 mM, stimulates Physcomitrium patens
1.8.4.9 additional information no iron is associated with recombinant PpPAPR Physcomitrium patens
1.8.4.10 (NH4)2SO4 activates Physcomitrium patens
1.8.4.10 KNO3 activates Physcomitrium patens
1.8.4.10 Mg2+ activates Physcomitrium patens
1.8.4.10 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
1.8.4.10 sulfate activates Physcomitrium patens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.4.9 32000
-
x * 32000, SDS-PAGE Physcomitrium patens
1.8.4.9 50000
-
x * 50000, recombinant His-tagged PpAPR, SDS-PAGE Physcomitrium patens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.9 adenylyl sulfate + glutathione Physcomitrium patens sulfate assimilation pathway in Physcomitrella patens, overview AMP + sulfite + glutathione disulfide
-
?
1.8.4.9 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 ?
-
?
1.8.4.10 adenylyl sulfate + thioredoxin Physcomitrium patens sulfate assimilation pathway in Physcomitrella patens, overview AMP + sulfite + thioredoxin disulfide
-
?
1.8.4.10 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

EC Number Organism UniProt Comment Textmining
1.8.4.9 Physcomitrium patens
-
-
-
1.8.4.10 Physcomitrium patens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.9 recombinant N-terminally His-tagged PpAPR from Escherichia coli Physcomitrium patens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.9 AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione 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 the C-terminal domain. In the third step, the glutaredoxin active site is regenerated by reduction with GSH reductase Physcomitrium patens
1.8.4.10 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

EC Number Storage Stability Organism
1.8.4.9 -20°C, 1 day, PpAPR is completely inactivated, plant APRs are very unstable enzymes because of the rapid loss of their iron-sulfur clusters Physcomitrium patens
1.8.4.9 -20°C, 1 day, PpAPR-B retains 30% of its activity Physcomitrium patens
1.8.4.9 4°C, PpAPR, completely stable for 48 h, inactivation after longer than 2 dayswith 15% remaining activity after 4-5 days Physcomitrium patens
1.8.4.9 4°C, PpAPR-B is stable over 5 days Physcomitrium patens
1.8.4.10 -20°C, 1 day, PpAPR-B retains 30% of its activity Physcomitrium patens
1.8.4.10 4°C, PpAPR-B, completely stable for 5 days Physcomitrium patens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.9 3'-phosphoadenosine 5'-phosphosulfate + dithioerythritol
-
Physcomitrium patens ?
-
?
1.8.4.9 3'-phosphoadenosine 5'-phosphosulfate + glutathione
-
Physcomitrium patens adenosine 3',5'-diphosphate + sulfite + oxidized glutathione
-
?
1.8.4.9 adenosine 5'-phosphosulfate + glutathione PpAPR-B is much more active with adenosine 5'-phosphosulfate as a substrate than with 3'-phosphoadenosine 5'-phosphosulfate Physcomitrium patens ?
-
?
1.8.4.9 adenylyl sulfate + DTT
-
Physcomitrium patens ?
-
?
1.8.4.9 adenylyl sulfate + glutathione sulfate assimilation pathway in Physcomitrella patens, overview Physcomitrium patens AMP + sulfite + glutathione disulfide
-
?
1.8.4.9 adenylyl sulfate + glutathione substrate binding structure, modelling, overview Physcomitrium patens AMP + sulfite + glutathione disulfide
-
?
1.8.4.9 additional information no activity with thioredoxin Physcomitrium patens ?
-
?
1.8.4.9 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 ?
-
?
1.8.4.10 adenylyl sulfate + thioredoxin sulfate assimilation pathway in Physcomitrella patens, overview Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?
1.8.4.10 adenylyl sulfate + thioredoxin dependent on thioredoxin, APS is the preferred substrate, substrate binding structure, modelling, overview Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?
1.8.4.10 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 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.8.4.9 ? x * 32000, SDS-PAGE Physcomitrium patens
1.8.4.9 ? x * 50000, recombinant His-tagged PpAPR, SDS-PAGE Physcomitrium patens

Synonyms

EC Number Synonyms Comment Organism
1.8.4.9 APR
-
Physcomitrium patens
1.8.4.9 PpAPR-B
-
Physcomitrium patens
1.8.4.10 APR
-
Physcomitrium patens
1.8.4.10 PpAPR-B
-
Physcomitrium patens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.9 37
-
-
Physcomitrium patens
1.8.4.10 37
-
-
Physcomitrium patens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.9 0.00075
-
3'-phosphoadenosine 5'-phosphosulfate
-
Physcomitrium patens
1.8.4.9 0.176
-
adenosine 5'-phosphosulfate
-
Physcomitrium patens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.9 7 8.5
-
Physcomitrium patens
1.8.4.9 8
-
substrate: 3'-phosphoadenosine 5'-phosphosulfate Physcomitrium patens
1.8.4.10 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
1.8.4.10 8
-
-
Physcomitrium patens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.9 glutathione
-
Physcomitrium patens
1.8.4.9 additional information FeS cluster as a cofactor in PpAPR, no activity with thioredoxin Physcomitrium patens
1.8.4.10 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
1.8.4.10 thioredoxin
-
Physcomitrium patens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8.4.9 0.176
-
adenosine 5'-phosphosulfate
-
Physcomitrium patens