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Transmitting the allosteric signal in methylglyoxal synthase

Falahati, Hanieh (author)
Pazhang, Mohammad (author)
Zareian, Shekufeh (author)
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Ghaemi, Nasser (author)
Rofougaran, Reza (author)
Hofer, Anders (author)
Umeå universitet,Institutionen för medicinsk kemi och biofysik
Rezaie, Alireza R (author)
Khajeh, Khosro (author)
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 (creator_code:org_t)
2013-04-16
2013
English.
In: Protein Engineering Design & Selection. - : Oxford University Press. - 1741-0126 .- 1741-0134. ; 26:7, s. 445-452
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • The homohexameric enzyme methylglyoxal synthase (MGS) converts dihydroxyacetone phosphate (DHAP) to methylglyoxal and phosphate. This enzyme is allosterically inhibited by phosphate. The allosteric signal induced by phosphate in MGS from Thermus sp. GH5 (TMGS) has been tracked by site-directed mutagenesis, from the binding site of phosphate to the pathways that transmit the signal, and finally to the active site which is the receiver of the signal. In TMGS, Ser-55 distinguishes the inhibitory phosphate from the phosphoryl group of the substrate, DHAP, and transmits the allosteric signal through Pro-82, Arg-97 and Val-101 to the active site. Furthermore, the addition of a C-terminal tail to TMGS reinforces the allosteric signal by introducing a new salt bridge between Asp-10 and an Arg in this tail. Lastly, the active site amino acid, Gly-56, is shown to be involved in both allostery and phosphate elimination step from DHAP by TMGS. Interestingly, some of the mutations also trigger homotropic allostery, supporting the hypothesis that allostery is an intrinsic property of all dynamic proteins. The details of the TMGS allosteric network discussed in this study can serve as a model system for understanding the enigmatic allosteric mechanism of other proteins.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

allosteric pathway
methylglyoxal synthase from Thermus sp. GH5 (TMGS)
mechanism of allostery
inhibition
triggered allostery

Publication and Content Type

ref (subject category)
art (subject category)

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