Steady-State Kinetic Analysis of Phosphotransacetylase from Methanosarcina thermophila
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چکیده
منابع مشابه
Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila.
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 ...
متن کاملAbstract No. Iyer367 Determination of the X-ray Crystal Structure of Phosphotransacetylase from Methanosarcina thermophila
No. Iyer367 Determination of the X-ray Crystal Structure of Phosphotransacetylase from Methanosarcina thermophila. P. Iyer, H. Yennawar (Penn State), K. Rajashankar (BNL, NSLS) and J. Ferry (Penn State) Beamline(s): X9A Introduction: Phosphotransacetylase is a key enzyme in the pathway of methanogenesis from acetate. In the archaeon Methanosarcina thermophila, phosphotransacetylase, along with ...
متن کاملFerry from Methanosarcina thermophila . phosphotransacetylase and acetate kinase hyperexpression of the genes encoding
from Methanosarcina thermophila. phosphotransacetylase and acetate kinase hyperexpression of the genes encoding Cloning, sequence analysis, and
متن کاملRole of arginines in coenzyme A binding and catalysis by the phosphotransacetylase from Methanosarcina thermophila.
Phosphotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA): CH(3)COOPO(3)(2-) + CoASH <==> CH(3)COSCoA + HPO(4)(2-). The role of arginine residues was investigated for the phosphotransacetylase from Methanosarcina thermophila. Kinetic analysis of a suite of variants indicated that Arg 87 and Arg 133 interact with the substr...
متن کاملStructural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila.
Phosphotransacetylase (EC 2.3.1.8) catalyzes reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. Two crystal structures of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila in complex with the substrate CoA revealed one CoA (CoA1) bound in the proposed active site cleft and an additional CoA...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2006
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.188.3.1155-1158.2006