Steady-State Kinetic Analysis of Phosphotransacetylase from Methanosarcina thermophila
2006 ◽
Vol 188
(3)
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pp. 1155-1158
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Keyword(s):
ABSTRACT Phosphotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. A steady-state kinetic analysis of the phosphotransacetylase from Methanosarcina thermophila indicated that there is a ternary complex kinetic mechanism rather than a ping-pong kinetic mechanism. Additionally, inhibition patterns of products and a nonreactive substrate analog suggested that the substrates bind to the enzyme in a random order. Dynamic light scattering revealed that the enzyme is dimeric in solution.
1975 ◽
Vol 250
(7)
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pp. 2709-2717
Keyword(s):
1991 ◽
Vol 266
(32)
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pp. 21616-21625
Keyword(s):
1981 ◽
Vol 256
(16)
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pp. 8845-8849
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Keyword(s):
1982 ◽
Vol 257
(2)
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pp. 924-929
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1991 ◽
Vol 266
(3)
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pp. 1516-1525
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Keyword(s):
1978 ◽
Vol 89
(1)
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pp. 203-212
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