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Literature summary for 2.7.7.51 extracted from

  • Wojdyla-Mamori, A.M.; Guranowski, A.
    Adenylylsulfate-ammonia adenylyltransferase activity is another inherent property of Fhit proteins (2015), Biosci. Rep., 35, e00235.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6
-
adenosine 5'-phosphorofluoridate pH 10.6, 30°C Homo sapiens
2.4
-
adenosine 5'-phosphosulfate pH 10.6, 30°C Homo sapiens
60
-
NH3 cosubstrate adenosine 5'-phosphorofluoridate, pH 10.6, 30°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O00298 cf. EC 3.6.1.29
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine 5'-phosphorofluoridate + NH3
-
Homo sapiens adenosine 5'-phosphoramidate + F-
-
?
adenosine 5'-phosphosulfate + NH3
-
Homo sapiens adenosine 5'-phosphoramidate + SO42- + H+
-
?
ApppA + NH3
-
Homo sapiens adenosine 5'-phosphoramidate + ppA
-
?
cytidine 5'-phosphosulfate + NH3 91% of the rate with adenosine 5'-phosphosulfate Homo sapiens cytidine 5'-phosphoramidate + SO42- + H+
-
?
guanosine 5'-phosphosulfate + NH3 47% of the rate with adenosine 5'-phosphosulfate Homo sapiens guanosine 5'-phosphoramidate + SO42- + H+
-
?
additional information enzyme catalyses ammonolysis of adenosine 5'-phosphosulfate, which results in the formation of adenosine 5'-phosphoramidate. The mechanism for Fhit-catalysed ammonolysis of these substrates most probably involves attack by NH3 on the covalent histidine-bound enzyme-nucleosidyl intermediate. No substrate: adenosine 5'-phosphosulfate-3-phosphate Homo sapiens ?
-
?
uridine 5'-phosphosulfate + NH3 56% of the rate with adenosine 5'-phosphosulfate Homo sapiens uridine 5'-phosphoramidate + SO42- + H+
-
?

Synonyms

Synonyms Comment Organism
diadenosine triphosphate hydrolase
-
Homo sapiens
Fhit
-
Homo sapiens
Fragile histidine triad protein
-
Homo sapiens