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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.

Word Map on EC 1.8.4.9

Reaction

AMP
+
sulfite
+
glutathione disulfide
=
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
                1.8.4.9 adenylyl-sulfate reductase (glutathione)

Crystallization

Crystallization on EC 1.8.4.9 - adenylyl-sulfate reductase (glutathione)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged C-terminal redox domain of AtAPR1, sitting drop vapor diffusion method, crystallization from 100 mM Tris, pH 7.0, 1.0 M sodium citrate, and 200 mM sodium chloride, at 10°C, 1 week, X-ray diffraction structure determination and analysis at 2.70 A resolution, structure modeling via molecular replacement method using the J-Trx1 fragment of protein disulfide reductase ERdj5 from Mus musculus (PDB entry 3APQ), as the template
hanging-drop vapour diffusion
-