Rationalization of allosteric pathway in Thermus sp. GH5 methylglyoxal synthase.
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ABSTRACT:
SUBMITTER: Zareian S
PROVIDER: S-EPMC4133812 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
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Rationalization of allosteric pathway in Thermus sp. GH5 methylglyoxal synthase.
Zareian Shekufeh S Khajeh Khosro K Pazhang Mohammad M Ranjbar Bijan B
BMB reports 20121201 12
A sequence of 10 amino acids at the C-terminus region of methylglyoxal synthase from Escherichia coli (EMGS) provides an arginine, which plays a crucial role in forming a salt bridge with a proximal aspartate residue in the neighboring subunit, consequently transferring the allosteric signal between subunits. In order to verify the role of arginine, the gene encoding MGS from a thermophile species, Thermus sp. GH5 (TMGS) lacking this arginine was cloned with an additional 30 bp sequence at the 3 ...[more]
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