Structure-activity studies of sulfate transfer: the hydrolysis and aminolysis of 3'-phosphoadenosine 5'-phosphosulfate (PAPS).

Abstract:

:The pH-rate profile for the hydrolysis of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in aqueous solution has been measured. Comparison with other data suggests that hydrolysis occurs by almost complete unimolecular elimination of sulfur trioxide, with weak involvement of a molecule of water in the transition state. The catalytic power (kcat/kuncat) of the sulfotransferases is estimated to be in the order of 10(10)-10(12). Amines--exemplified by morpholine--react spontaneously with PAPS in water at 39 degrees C by attack at both sulfuryl and (5')phosphoryl groups in a ratio of 2:3. The mechanism of activation of the coenzyme, PAPS, by the sulfotransferases that catalyse N-sulfation must involve suppression of its native N-phosphorylating reactivity and specific enhancement of its N-sulfating reactivity. Studies of the aminolysis of the coenzyme in aprotic solvent-water mixtures suggest how this might be accomplished.

journal_name

Bioorg Med Chem

authors

Bedford CT,Kirby AJ,Logan CJ,Drummond JN

doi

10.1016/0968-0896(95)00015-9

subject

Has Abstract

pub_date

1995-02-01 00:00:00

pages

167-72

issue

2

eissn

0968-0896

issn

1464-3391

pii

0968089695000159

journal_volume

3

pub_type

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