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Literature summary for 2.7.7.4 extracted from

  • Deyrup, A.T.; Singh, B.; Krishnan, S.; Lyle, S.; Schwartz, N.B.
    Chemical modification and site-directed mutagenesis of conserved HXXH and PP-loop motif arginines and histidines in the murine bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase (1999), J. Biol. Chem., 274, 28929-28936.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D523A no sulfurylase activity, reduced PAPS kinase activity Mus musculus
H425A no sulfurylase activity Mus musculus
H428A no sulfurylase activity Mus musculus
H506A mutant enzyme shows 91% of the sulfurylase activity compared to that of the wild-type enzyme, reduced PAPS kinase activity Mus musculus
R421A no sulfurylase activity Mus musculus
R421K mutant enzyme shows 8% of the sulfurylase activity compared to that of the wild-type enzyme Mus musculus
R468A no sulfurylase activity Mus musculus
R510A mutant enzyme shows 90% of the sulfurylase activity compared to that of the wild-type enzyme Mus musculus
R522A no sulfurylase activity Mus musculus
R522K no sulfurylase activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
-

Source Tissue

Source Tissue Comment Organism Textmining
chondrosarcoma cell
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + sulfate
-
Mus musculus diphosphate + adenylylsulfate
-
r