Open AccessPurification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate‐reducer, Archaeoglobus fulgidus
Author(s) -
Dahl Christiane,
Koch HansGeorg,
Keuken Oliver,
Trüper Hans G.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb13830.x
Subject(s) - thermophile , ammonium sulfate , chemistry , enzyme , size exclusion chromatography , biochemistry , chromatography , fractionation , fast protein liquid chromatography
ATP sulfurylase (sulfate adenylyltransferase, EC 2.7.7.4) was isolated from the recently described extremely thermophilic sulfate‐reducing archaebacterium Archaeglobus fulgidus . The enzyme was purified by ammonium sulfate fractionation and FPLC on Phenyl‐Sepharose Fast Flow, Mono‐Q and Superose 6. The M r of ATP sulfurylase was estimated at 150 000 by analytical gel filtration on Superose 6. The enzyme exhibited a strong tendency to form catalytically active trimers. The enzyme preparation gave two bands with molecular weights of 50 000 and 53 000 on analysis of SDS‐PAGE, suggesting an α 2 β structure of the monomer. The pH‐optimum for activity was 8.0 and the optimum reaction temperature was 90°C. The apparent K m values for adenylylsulfate and yrophosphate were 0.17 mM and 0.13 mM, respectively. The p I of the archaebacterial ATP sulfurylase was 4.3.