Affiliation:
1. Department of Bacteriology, University of Kansas, Lawrence, Kansas
2. Department of Microbiology, School of Medicine, Western Reserve University, Cleveland, Ohio
Abstract
Akagi
, J. M. (University of Kansas, Lawrence)
and L. Leon Campbell
. Studies on thermophilic sulfate-reducing bacteria. III. Adenosine triphosphate-sulfurylase of
Clostridium nigrificans
and
Desulfovibrio desulfuricans
. J. Bacteriol.
84:
1194–1201. 1962.—Adenosine triphosphate (ATP)-sulfurylase, which catalyzes the formation of adenosine-5′-phosphosulfate (APS) from ATP and SO
4
=
, has been purified from crude extracts of
Clostridium nigrificans
and
Desulfovibrio desulfuricans
by (NH
4
)
2
SO
4
fractionation and triethylaminoethyl column chromatography. The enzyme from both sources operates over a broad pH range from 6.0 to 9.5. Below pH 6.0, activity decreases sharply, with no detectable activity at pH 5.0. Of the nucleotides tested (ATP and the triphosphates of deoxyadenosine, uridine, inosine, and guanosine), only ATP was acted upon by the enzyme from either source. The enzyme requires Mg
++
for activity. Incubation of the enzyme from both organisms with ATP and S
35
O
4
=
in the presence of helium resulted in the formation of an S
35
-labeled nucleotide whose electrophoretic mobility was identical to that of chemically prepared APS. When incubated with ATP and the group VI anions (CrO
4
, MoO
4
, WO
4
), the enzyme from both organisms formed an unstable intermediate, resulting in the accumulation of pyrophosphate. Thermal stability studies revealed that the ATP-sulfurylase of
C. nigrificans
was stable at higher temperatures than the enzyme obtained from
D. desulfuricans
. Exposure of the enzyme from
C. nigrificans
to 65 C for 2 hr gave virtually no decrease in activity. In contrast, the enzyme from
D. desulfuricans
was completely inactivated after 30 min at 55 C, after 3 min at 60 C, or after 1 min at 65 C.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference29 articles.
1. Studies on thermophilic sulfate-reducing bacteria. II. Hydrogenase activity of Clostridium nigrificans;AKAGI J.;J. Bacteriol.,1961
2. AKAGI J. M. AND L. L. CAMPBELL. 1962. Studies on thermophilic sulfate-reducing bacteria. III. ATP-sulfurylase of Clostridtum nigrificans and Desulfovibrio desulfuricans. Bacteriol. Proc. p. 102.
3. Synthesis of adenosine-5'-sulphatophosphate. A degradation product of an intermediate in the enzymatic synthesis of sulphuric esters;BADDILEY J., J.;J. Chem. Soc., p.,1957
4. Choline fermentation by Desulfovibrio desulfuricans;BAKER F. D.;J. Bacteriol.,1962
5. The mechanism of "active sulfate;BANDURSKI R. S.;J. Am. Chem. Soc.,1956
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