Abstract
ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus is a bacterial ortholog of the enzyme from filamentous fungi. (The subunit contains an adenosine 5′-phosphosulfate (APS) kinase-like, C-terminal domain.) The enzyme is highly heat stable with a half-life > 1 h at 90°C. Steady-state kinetics are consistent with a random A-B, ordered P-Q mechanism where A = MgATP, B = SO2- 4, P = PPi, and Q = APS. The kinetic constants suggest that the enzyme is optimized to act in the direction of ATP + sulfate formation. Chlorate is competitive with sulfate and with APS. In sulfur chemolithotrophs, ATP sulfurylase provides an efficient route for recycling PPi produced by biosynthetic reactions. However, the protein possesses low APS kinase activity. Consequently, it may also function to produce PAPS for sulfate ester formation or sulfate assimilation when hydrogen serves as the energy source and a reduced inorganic sulfur source is unavailable.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 275-288 |
| Number of pages | 14 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 406 |
| Issue number | 2 |
| DOIs | |
| State | Published - 2002 |
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Keywords
- Adenylylsulfate (APS) kinase, from Aquifex aeolicus, hyperthermophile, ATP sulfurylase from
- ATP sulfurylase, from Aquifex aeolicus
- Chemolithotroph, ATP sulfurylase, and APS kinase in
- Sulfurylase, from a hyperthermophilic bacterium
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus. / Hanna, Eissa; MacRae, Ian J.; Medina, Daniel C.; Fisher, Andrew J; Segel, Irwin H.
In: Archives of Biochemistry and Biophysics, Vol. 406, No. 2, 2002, p. 275-288.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus
AU - Hanna, Eissa
AU - MacRae, Ian J.
AU - Medina, Daniel C.
AU - Fisher, Andrew J
AU - Segel, Irwin H.
PY - 2002
Y1 - 2002
N2 - ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus is a bacterial ortholog of the enzyme from filamentous fungi. (The subunit contains an adenosine 5′-phosphosulfate (APS) kinase-like, C-terminal domain.) The enzyme is highly heat stable with a half-life > 1 h at 90°C. Steady-state kinetics are consistent with a random A-B, ordered P-Q mechanism where A = MgATP, B = SO2- 4, P = PPi, and Q = APS. The kinetic constants suggest that the enzyme is optimized to act in the direction of ATP + sulfate formation. Chlorate is competitive with sulfate and with APS. In sulfur chemolithotrophs, ATP sulfurylase provides an efficient route for recycling PPi produced by biosynthetic reactions. However, the protein possesses low APS kinase activity. Consequently, it may also function to produce PAPS for sulfate ester formation or sulfate assimilation when hydrogen serves as the energy source and a reduced inorganic sulfur source is unavailable.
AB - ATP sulfurylase from the hyperthermophilic chemolithotroph Aquifex aeolicus is a bacterial ortholog of the enzyme from filamentous fungi. (The subunit contains an adenosine 5′-phosphosulfate (APS) kinase-like, C-terminal domain.) The enzyme is highly heat stable with a half-life > 1 h at 90°C. Steady-state kinetics are consistent with a random A-B, ordered P-Q mechanism where A = MgATP, B = SO2- 4, P = PPi, and Q = APS. The kinetic constants suggest that the enzyme is optimized to act in the direction of ATP + sulfate formation. Chlorate is competitive with sulfate and with APS. In sulfur chemolithotrophs, ATP sulfurylase provides an efficient route for recycling PPi produced by biosynthetic reactions. However, the protein possesses low APS kinase activity. Consequently, it may also function to produce PAPS for sulfate ester formation or sulfate assimilation when hydrogen serves as the energy source and a reduced inorganic sulfur source is unavailable.
KW - Adenylylsulfate (APS) kinase, from Aquifex aeolicus, hyperthermophile, ATP sulfurylase from
KW - ATP sulfurylase, from Aquifex aeolicus
KW - Chemolithotroph, ATP sulfurylase, and APS kinase in
KW - Sulfurylase, from a hyperthermophilic bacterium
UR - http://www.scopus.com/inward/record.url?scp=0036403872&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036403872&partnerID=8YFLogxK
U2 - 10.1016/S0003-9861(02)00428-9
DO - 10.1016/S0003-9861(02)00428-9
M3 - Article
C2 - 12361716
AN - SCOPUS:0036403872
VL - 406
SP - 275
EP - 288
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -