Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.4 extracted from

  • Deyrup, A.T.; Krishnan, S.; Cockburn, B.N.; Schwartz, N.B.
    Deletion and site-directed mutagenesis of the ATP-binding motif (P-loop) in the bifunctional murine ATP-sulfurylase/adenosine 5'-phosphosulfate kinase enzyme (1998), J. Biol. Chem., 273, 9450-9456.
    View publication on PubMed
Search for more literature for 2.7.7.4

Protein Variants

Protein Variants Comment Organism
C53A mutation has no effect on activity Mus musculus
C77A mutation has no effect on activity Mus musculus
C84A mutation has no effect on activity Mus musculus
G59A significant effect on ATP sulfurylase activity, no effect on adenosine 5'-phosphosulfate kinase activity Mus musculus
G62A mutation has no effect on activity Mus musculus
G64A diminished adenosine 5'-phosphosulfate kinase activity Mus musculus
K65A mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact Mus musculus
K65R mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact Mus musculus
T66A mutation ablates adenosine 5'-phosphosulfate kinase activity while leaving ATP sulfurylase activity intact Mus musculus

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
 synthesis of ATP, enzyme form ATPSm and ATPSc Mus musculus