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Literature summary for 1.8.4.9 extracted from

  • Bick, J.A.; Aeslund, F.; Chen, Y.; Leustek, T.
    Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase (1998), Proc. Natl. Acad. Sci. USA, 95, 8404-8409.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.9

Cloned(Commentary)

Cloned (Comment) Organism
gene APR1, expression of the holoenzyme APR1p in Escherichia coli strain BL21(DE3), separate expression in Escherichia coli strain BL21(DE3) of amino acid residues 73-327, forming the R-domain, and of residues 328-465, forming the C-domain, the domains alone are inactive, but mixing of both can partially restore activity Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information gene APR1, the holoenzyme APR1p as well as the C-domain alone can complement the cysteine auxotrophy of an Escherichia coli cysH mutant strain, substituting for glutaredoxin, if the mutant is capable of producing glutathione, cysH encodes the 5'-phosphoadenylylsulfate reductase in Escherichia coli Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
glutathione slightly inhibitory at high concentrations Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
 glutathione holoenzyme APR1p with substrate 5'-adenylyl sulfate, pH 8.5, 30°C Arabidopsis thaliana
1.12
-
 glutathione about, holoenzyme APR1p and C-domain with substrates hydroxyethyldisulfide, or cystine, pH 8.0, 24°C Arabidopsis thaliana
1.15
-
 glutathione about, holoenzyme APR1p and C-domain with substrate dehydroascorbate, pH 6.9, 24°C Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana enzyme is involved in sulfate assimilation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P92979 APR1; 3 genes APR1, APR2, and APR3, 3 isozymes APR1p, APR2p, and APR3p
-

Purification (Commentary)

Purification (Comment) Organism
recombinant holoenzyme APR1p, C-domain, and R-domain from Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-adenylyl sulfate + glutathione catalyzed by the holoenzyme APR1p, not by the C-domain Arabidopsis thaliana AMP + sulfite + glutathione disulfide
-
 ?
cystine + glutathione catalyzed by the holoenzyme APR1p and the C-domain Arabidopsis thaliana cysteine + glutathione disulfide
-
 ?
dehydroascorbate + glutathione catalyzed by the holoenzyme APR1p and the C-domain Arabidopsis thaliana ascorbate + glutathione disulfide
-
 ?
hydroxyethyldisulfide + glutathione catalyzed by the holoenzyme APR1p and the C-domain Arabidopsis thaliana ?
-
 ?
insulin disulfide + glutathione catalyzed by the C-domain, not by the holoenzyme APR1p or the R-domain Arabidopsis thaliana insulin + glutathione disulfide
-
 ?
additional information enzyme is involved in sulfate assimilation Arabidopsis thaliana ?
-
 ?
oxidized ribonucleotide reductase + glutathione catalyzed by the C-domain, not by the holoenzyme APR1p or the R-domain Arabidopsis thaliana reduced ribonucleotide reductase + glutathione disulfide
-
 ?

Subunits

Subunits Comment Organism
More amino acid residues 73-327 form the R-domain which is homologous to microbial 5'-phosphoadenylylsulfate reductase, and of residues 328-465 form the C-domain which is homologous to thioredoxin, the domains alone are inactive, but mixing of both can partially rstore activity Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
5'-adenylylsulfate reductase
-
 Arabidopsis thaliana
APR1p
-
 Arabidopsis thaliana
APS reductase
-
 Arabidopsis thaliana
More enzyme belongs to the thioredoxin superfamily Arabidopsis thaliana
plant-type 5'-adenylylsulfate reductase
-
 Arabidopsis thaliana

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
24 30
-
 Arabidopsis thaliana

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5
-
 Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
glutathione dependent on, specific cofactor for the carboxyterminal glutathione-dependent reductase domain of the enzyme, can be exchanged for equally active DTT, glutathione is slightly inhibitory at high concentrations Arabidopsis thaliana
additional information DTT can be exchanged for glutathione, equally active Arabidopsis thaliana
additional information no activity with 2-mercaptoethanol, gamma-glutamylcysteine, or cysteine Arabidopsis thaliana