Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1

Definition:

Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells.

References:

[1]. J P Girard, et al. Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [Content Brief]

[2]. Stefan Harjes, et al. Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):350-2. [Content Brief]

[3]. K Yanagisawa, et al. cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [Content Brief]

[4]. K V Venkatachalam, et al. Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [Content Brief]

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