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Literature summary extracted from

  • Wiedemann, G.; Koprivova, A.; Schneider, M.; Herschbach, C.; Reski, R.; Kopriva, S.
    The role of the novel adenosine 5-phosphosulfate reductase in regulation of sulfate assimilation of Physcomitrella patens (2007), Plant Mol. Biol., 65, 667-676.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.9 APR, DNA and amino acid sequence determination and analysis, semiquantitative expression analysis, overexpression of His-tagged APR isozyme in Escherichia coli Physcomitrium patens
1.8.4.10 APR-B, DNA and amino acid sequence determination and analysis, semiquantitative expression analysis, overexpression of His-tagged APR-B isozyme in Escherichia coli Physcomitrium patens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.9 additional information construction of APR-B knockout plants, the mutant plants are able to grow on sulfate as a sole sulfur source, and the content of low molecular weight thiols is not different from wild-type plants. However, when treated with low concentrations of cadmium, the APR-B knockout plants are more sensitive than wild-type plants, phenotype, overview Physcomitrium patens
1.8.4.10 additional information construction of APR-B knockout plants, the mutant plants are able to grow on sulfate as a sole sulfur source, and the content of low molecular weight thiols is not different from wild-type plants. However, when treated with low concentrations of cadmium, the APR-B knockout plants are more sensitive than wild-type plants, phenotype, overview Physcomitrium patens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.9 Fe2+ APR contains a FeS cluster Physcomitrium patens
1.8.4.9 Mg2+
-
Physcomitrium patens
1.8.4.10 Mg2+
-
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
-
AMP + sulfite + glutathione disulfide
-
?
1.8.4.10 adenylyl sulfate + thioredoxin Physcomitrium patens in Physcomitrella patens, APS reduction is not the major control step of sulfate assimilation AMP + sulfite + thioredoxin disulfide
-
?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.9 adenylyl sulfate + DTT
-
Physcomitrium patens ?
-
?
1.8.4.9 adenylyl sulfate + glutathione
-
Physcomitrium patens AMP + sulfite + glutathione disulfide
-
?
1.8.4.10 adenylyl sulfate + thioredoxin
-
Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?
1.8.4.10 adenylyl sulfate + thioredoxin in Physcomitrella patens, APS reduction is not the major control step of sulfate assimilation Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.9 9
-
assay at Physcomitrium patens
1.8.4.10 9
-
assay at Physcomitrium patens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.9 glutathione
-
Physcomitrium patens
1.8.4.9 additional information APR contains a FeS cluster 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 Physcomitrium patens
1.8.4.10 thioredoxin
-
Physcomitrium patens