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Literature summary for 2.7.7.4 extracted from

  • Shaw, W.H.; Anderson, J.W.
    Purification, properties and substrate specificity of adenosine triphosphate sulphurylase from spinach leaf tissue (1972), Biochem. J., 127, 237-247.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.35
-
ATP pH 7.8, 35°C Spinacia oleracea
0.84
-
dATP pH 7.8, 35°C Spinacia oleracea
1
-
SeO42- pH 7.8, 35°C Spinacia oleracea
3.1
-
SO42- pH 7.8, 35°C Spinacia oleracea

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Mg2+ or Co2+ required Spinacia oleracea
Mg2+ Mg2+ or Co2+ required Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Storage Stability

Storage Stability Organism
-15°C, stable for at least 4 months Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + SeO42-
-
Spinacia oleracea AMP + adenylylselenate
-
?
ATP + sulfate
-
Spinacia oleracea diphosphate + adenylylsulfate
-
r
dATP + SO42-
-
Spinacia oleracea diphosphate + deoxyadenylylsulfate
-
?
additional information sulfate is the only form of sulfur that catalyzes diphosphate-ATP exchange. The enzyme catalyzes diphosphate-dATP exchange. Selenate catalyzes diphosphate-ATP exchange, but no AMP is formed. Molybdate does not catalyze diphosphate-ATP exchange but AMP is formed Spinacia oleracea ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
1 min, complete loss of activity Spinacia oleracea

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9
-
Spinacia oleracea