Literature summary for 2.7.1.25 extracted from

Deyrup, A.T.; Krishnan, S.; Singh, B.; Schwartz, N.B.
Activity and stability of recombinant bifunctional rearranged and monofunctional domains of ATP-sulfurylase and adenosine 5'-phosphosulfate kinase (1999), J. Biol. Chem., 274, 10751-10757.

Search for more literature for 2.7.1.25

Cloned(Commentary)

Cloned (Comment)	Organism
expresssion in Escherichia coli	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.00016	-	recombinant enzyme	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + adenosine 5-phosphosulfate	i.e. adenylylsulfate or APS	Mus musculus	ADP + 3'-phosphoadenosine 5'-phosphosulfate	i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
37	-	no loss of activity after 2 h, recombinant enzyme	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)