APSe is phosphorylated to PAPSe by PAPSS1,2

Stable Identifier
Homo sapiens
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Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthases 1 and 2 (PAPSS1,2) (Venkatachalam et al. 1998, Xu et al. 2000) are involved in phosphorylating adenylylselenate (APSe) into 3'-phosphoadenylyl selenate (PAPSe) via its APS kinase domain. This reaction is inferred from the event in Penicillium chrysogenum involving APS kinase (Kaps) (Yu et al. 1989).

Literature References
PubMed ID Title Journal Year
9668121 Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains

Venkatachalam, KV, Akita, H, Strott, CA

J Biol Chem 1998
10679223 Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization

Xu, JP, Kim, UJ, Freimuth, RR, Mitchell, S, Moon, E, Otterness, DM, Wood, TC, Xu, ZH, Carlini, EJ, Weinshilboum, RM, Siciliano, MJ

Biochem. Biophys. Res. Commun. 2000
2537056 Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions

Chen, LJ, Segel, IH, Yu, M, Martin, RL, Jain, S

Arch. Biochem. Biophys. 1989
Catalyst Activity

adenylylselenate kinase activity of PAPSS1,2 [cytosol]

Inferred From
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