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Literature summary extracted from

  • Stevenson, C.E.; Hughes, R.K.; McManus, M.T.; Lawson, D.M.; Kopriva, S.
    The X-ray crystal structure of APR-B, an atypical adenosine 5-phosphosulfate reductase from Physcomitrella patens (2013), FEBS Lett., 587, 3626-3632 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.4.10 crystal structure is consistent with a preference for adenosine 5'-phosphosulfate. The [Fe4-S4] cluster enhances the enzyme's activity Physcomitrium patens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.10 D122G mutant does not display improved activity with 3'-phosphoadenosine-5'-phosphosulfate and shows significantly reduced activity with 5'-adenylylsulfate as the substrate Physcomitrium patens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.10 0.0058
-
5'-adenylyl sulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.0069
-
5'-adenylyl sulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.04
-
3'-phosphoadenosine-5'-phosphosulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.049
-
3'-phosphoadenosine-5'-phosphosulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.4.10 64000
-
gel filtration Physcomitrium patens
1.8.4.10 71000
-
dynamic light scattering Physcomitrium patens

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.10 Physcomitrium patens Q8L5D0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.10 3'-phosphoadenosine-5'-phosphosulfate + thioredoxin substrate of phosphoadenylyl-sulfate reductase, EC 1.8.4.8 Physcomitrium patens ? + thioredoxin disulfide
-
?
1.8.4.10 5'-adenylyl sulfate + thioredoxin
-
Physcomitrium patens AMP + sulfite + thioredoxin disulfide
-
?

Subunits

EC Number Subunits Comment Organism
1.8.4.10 dimer crystallization data Physcomitrium patens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.10 0.0001
-
3'-phosphoadenosine-5'-phosphosulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.0002
-
3'-phosphoadenosine-5'-phosphosulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.015
-
5'-adenylyl sulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.333
-
5'-adenylyl sulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.10 [4Fe-4S]-center
-
Physcomitrium patens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.4.10 0.0034
-
3'-phosphoadenosine-5'-phosphosulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 0.0037
-
3'-phosphoadenosine-5'-phosphosulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 2.6
-
5'-adenylyl sulfate mutant D122G, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens
1.8.4.10 48.3
-
5'-adenylyl sulfate wild-type, pH not specified in the publication, temperature not specified in the publication Physcomitrium patens