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Literature summary for 2.7.1.25 extracted from

  • Venkatachalam, K.V.; Akita, H.; Strott, C.A.
    Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains (1998), J. Biol. Chem., 273, 19311-19320.
    View publication on PubMed
Search for more literature for 2.7.1.25

Cloned(Commentary)

Cloned (Comment) Organism
expression of full-length PAPS synthase and 1-268 N-terminal fragment in COS-1 cells and Escherichia coli Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
 adenosine 5'-phosphosulfate pH 8.0, 37°C, COS-1 cell-expressed full length PAPS synthase Homo sapiens
0.0006
-
 adenosine 5'-phosphosulfate pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment Homo sapiens
0.0023
-
 adenosine 5'-phosphosulfate pH 8.0, 37°C, Escherichia coli-expressed N-terminal fragment Homo sapiens
0.0026
-
 adenosine 5'-phosphosulfate pH 8.0, 37°C, Escherichia coli-expressed full length PAPS synthase Homo sapiens
0.23
-
 ATP pH 8.0, 37°C, COS-1 cell-expressed N-terminal fragment Homo sapiens
0.26
-
 ATP pH 8.0, 37°C, E. coli expressed N-terminal fragment Homo sapiens
0.45
-
 ATP pH 8.0, 37°C, E. coli-expressed full length PAPS synthase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O43252 bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + adenosine 5-phosphosulfate enzyme has both ATP sulfurylase and APS kinase activity Homo sapiens ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate ?
ATP + adenosine 5-phosphosulfate i.e. adenylylsulfate or APS Homo sapiens ADP + 3'-phosphoadenosine 5'-phosphosulfate i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate ?

Synonyms

Synonyms Comment Organism
PAPS synthase
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-