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1.8.4.9: adenylyl-sulfate reductase (glutathione)

This is an abbreviated version!
For detailed information about adenylyl-sulfate reductase (glutathione), go to the full flat file.

Wordmap for 1.8.4.9

Word Map on EC 1.8.4.9 Wordmap for 1.8.4.9

Reaction

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AMP
+
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sulfite
+
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glutathione disulfide
=
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adenylyl sulfate
+ 2 glutathione

Synonyms

3'-phosphoadenosine-5'-phosphosulfate reductase homolog 19, 3'-phosphoadenosine-5'-phosphosulfate reductase homolog 26, 3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43, 5'-adenylylsulfate reductase, 5-adenosinephosphosulphate reductase, adenosine 5'-phosphosulfate reductase, adenosine 5-phosphosulfate reductase, adenosine-5'-phosphosulfate reductase, adenosine-5'-phosphosulphate reductase, APR, APR1, APR1p, APR2, APS reductase, At1g62180, AtAPR1, CysH, EC 1.8.99.2, EiAPR, More, PAPS reductase homolog 19, PAPS reductase homolog 26, PAPS reductase homolog 43, plant-type 5'-adenylylsulfate reductase, PpAPR-B, Prh-19, Prh-26, Prh-43

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.4 With a disulfide as acceptor
                EC 1.8.4.91.8.4.9 adenylyl-sulfate reductase (glutathione)

Temperature Stability

Temperature Stability on EC 1.8.4.9 - adenylyl-sulfate reductase (glutathione)

for references in articles please use BRENDA:EC1.8.4.9

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
thermal denaturation of the AtAPR1 redox domain presents a highly thermoreversible property, melting temperature can be roughly estimated as 55┬░C. The secondary structure of the redox domain is greatly distorted on heating to 55┬░C by estimating from a series of CD spectra at various temperatures. The CD spectra for the AtAPR1 redox domain, which is 95┬░C thermal-denatured followed by cooling to 25┬░C, is almost identical to that of the native AtAPR1 redox domain measured at 25┬░C. This indicates that thermal denaturation of the redox domain is reversible