Analysis of a dual domain phosphoglycosyl transferase reveals a ping-pong mechanism with a covalent enzyme intermediate
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چکیده
منابع مشابه
Analysis of a dual domain phosphoglycosyl transferase reveals a ping-pong mechanism with a covalent enzyme intermediate.
Phosphoglycosyl transferases (PGTs) are integral membrane proteins with diverse architectures that catalyze the formation of polyprenol diphosphate-linked glycans via phosphosugar transfer from a nucleotide diphosphate-sugar to a polyprenol phosphate. There are two PGT superfamilies that differ significantly in overall structure and topology. The polytopic PGT superfamily, represented by MraY a...
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Succinyl coenzyme A synthetase from Escherichia coli does not exhibit a steady state kinetic pattern indicative of “ping-pong” kinetics, despite the fact that catalytic participation of a phosphorylated enzyme covalent intermediate has been established. Instead, kineti.c patterns are consistent with the sequential addition of all substrates, to form a quaternary complex, before the release of a...
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Acyl-transfer catalysed by y-glutamyltranspeptidase from bovine kidney was studied using y-Land y-D-Glu-p-nitroanilide as the donor and GlyGly as the acceptor. The transfer of the y-Glu group to GlyGly was shown to be accompanied by transfer of the y-Glu group to water (hydrolysis). The results were compared with acyl-transfer catalysed by the representative serine protease, a-chymotrypsin. The...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2017
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1703397114