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Literature summary 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

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

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.4 chondrosarcoma cell
-
 Mus musculus
-

Substrates and Products (Substrate)

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