Abstract
The Thiobacillus denitrificans genome contains two sequences corresponding to ATP sulfurylase (Tbd_0210 and Tbd_0874). Both genes were cloned and expressed protein characterized. The larger protein (Tbd_0210; 544 residues) possesses an N-terminal ATP sulfurylase domain and a C-terminal APS kinase domain and was therefore annotated as a bifunctional enzyme. But, the protein was not bifunctional because it lacked ATP sulfurylase activity. However, the enzyme did possess APS kinase activity and displayed substrate inhibition by APS. Truncated protein missing the N-terminal domain had <2% APS kinase activity suggesting the function of the inactive sulfurylase domain is to promote the oligomerization of the APS kinase domains. The smaller gene product (Tbd_0874; 402 residues) possessed strong ATP sulfurylase activity with kinetic properties that appear to be kinetically optimized for the direction of APS utilization and ATP + sulfate production, which is consistent with an enzyme that functions physiologically to produce inorganic sulfate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 110-117 |
| Number of pages | 8 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 489 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Sep 2009 |
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Keywords
- APS kinase, from Thiobacillus
- ATP sulfurylase, from Thiobacillus
- Chemolithotrophic
- Enzyme kinetics
- Kinase, APS, from Thiobacillus
- Sulfate activating enzyme, from Thiobacillus
- Sulfate formation, by Thiobacillus
- Sulfate metabolism
- Sulfurylase, ATP, from Thiobacillus
- Thiobacillus denitrificans, ATP sulfurylase, from Thiobacillus
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Kinetic properties of ATP sulfurylase and APS kinase from Thiobacillus denitrificans. / Gay, Sean C.; Fribourgh, Jennifer L.; Donohoue, Paul D.; Segel, Irwin H.; Fisher, Andrew J.
In: Archives of Biochemistry and Biophysics, Vol. 489, No. 1-2, 09.2009, p. 110-117.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Kinetic properties of ATP sulfurylase and APS kinase from Thiobacillus denitrificans
AU - Gay, Sean C.
AU - Fribourgh, Jennifer L.
AU - Donohoue, Paul D.
AU - Segel, Irwin H.
AU - Fisher, Andrew J
PY - 2009/9
Y1 - 2009/9
N2 - The Thiobacillus denitrificans genome contains two sequences corresponding to ATP sulfurylase (Tbd_0210 and Tbd_0874). Both genes were cloned and expressed protein characterized. The larger protein (Tbd_0210; 544 residues) possesses an N-terminal ATP sulfurylase domain and a C-terminal APS kinase domain and was therefore annotated as a bifunctional enzyme. But, the protein was not bifunctional because it lacked ATP sulfurylase activity. However, the enzyme did possess APS kinase activity and displayed substrate inhibition by APS. Truncated protein missing the N-terminal domain had <2% APS kinase activity suggesting the function of the inactive sulfurylase domain is to promote the oligomerization of the APS kinase domains. The smaller gene product (Tbd_0874; 402 residues) possessed strong ATP sulfurylase activity with kinetic properties that appear to be kinetically optimized for the direction of APS utilization and ATP + sulfate production, which is consistent with an enzyme that functions physiologically to produce inorganic sulfate.
AB - The Thiobacillus denitrificans genome contains two sequences corresponding to ATP sulfurylase (Tbd_0210 and Tbd_0874). Both genes were cloned and expressed protein characterized. The larger protein (Tbd_0210; 544 residues) possesses an N-terminal ATP sulfurylase domain and a C-terminal APS kinase domain and was therefore annotated as a bifunctional enzyme. But, the protein was not bifunctional because it lacked ATP sulfurylase activity. However, the enzyme did possess APS kinase activity and displayed substrate inhibition by APS. Truncated protein missing the N-terminal domain had <2% APS kinase activity suggesting the function of the inactive sulfurylase domain is to promote the oligomerization of the APS kinase domains. The smaller gene product (Tbd_0874; 402 residues) possessed strong ATP sulfurylase activity with kinetic properties that appear to be kinetically optimized for the direction of APS utilization and ATP + sulfate production, which is consistent with an enzyme that functions physiologically to produce inorganic sulfate.
KW - APS kinase, from Thiobacillus
KW - ATP sulfurylase, from Thiobacillus
KW - Chemolithotrophic
KW - Enzyme kinetics
KW - Kinase, APS, from Thiobacillus
KW - Sulfate activating enzyme, from Thiobacillus
KW - Sulfate formation, by Thiobacillus
KW - Sulfate metabolism
KW - Sulfurylase, ATP, from Thiobacillus
KW - Thiobacillus denitrificans, ATP sulfurylase, from Thiobacillus
UR - http://www.scopus.com/inward/record.url?scp=69849111499&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=69849111499&partnerID=8YFLogxK
U2 - 10.1016/j.abb.2009.07.026
DO - 10.1016/j.abb.2009.07.026
M3 - Article
C2 - 19664586
AN - SCOPUS:69849111499
VL - 489
SP - 110
EP - 117
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1-2
ER -