1.8.4.9: adenylyl-sulfate reductase (glutathione)

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For detailed information about adenylyl-sulfate reductase (glutathione), go to the full flat file.

Reaction

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)

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Results	in table
6	Activating Compound
17	AA Sequence
2	Application
1	CAS Registry Number
16	Cloned(Commentary)
13	Cofactor
3	Crystallization (Commentary)
3	Expression
13	General Information
2	General Stability
11	Inhibitors
4	Ki Value [mM]
25	KM Value [mM]
9	Localization
11	Metals/Ions
20	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
59	Organism
7	Pathway
1	PDB ID
6	pH Optimum
1	pH Range
7	Protein Variants
9	Purification (Commentary)
2	Reaction
3	Reaction Type
34	Reference
13	Source Tissue
23	Specific Activity [micromol/min/mg]
4	Storage Stability
71	Substrates and Products (Substrate)
9	Subunits
56	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
11	Turnover Number [1/s]

Temperature Stability

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

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

Arabidopsis thaliana

P92979

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

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