title: Conferral of allostery to Thermus sp. GH5 methylglyoxal synthase by a single mutation.
abstract: There is huge number of oligomeric proteins that show allosteric behaviour as soon as their allosteric effector is provided. Thermus sp. GH5 methylglyoxal synthase is also a homohexameric protein, which displays cooperative behaviour when phosphate concentration increases. Previous studies on this enzyme have indicated that binding of phosphate leads to formation of specific interactions which makes the enzyme capable of displaying allosteric behaviour when its substrate is bound. In this study, it has been shown that a single mutation, independent of phosphate, provides the requirements for showing such cooperative behaviour. However, it is proposed that the allosteric mechanism triggered by phosphate is different from that applied by the mutation. These findings point towards the fact that allostery can be acquired, modulated or eliminated by any alteration in structure and/or dynamics of the proteins and all proteins are potentially capable of showing cooperative behaviour as soon as their prerequisites for this phenomenon are provided by the allosteric effector.
authors.affiliation: Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran 14115-175, Iran.
authors.forename: Zohreh
authors.initials: Z
authors.lastname: Farsi
authors.forename: Helmut
authors.initials: H
authors.lastname: Pein
authors.forename: Mohammad
authors.initials: M
authors.lastname: Pazhang
authors.forename: Shekufeh
authors.initials: S
authors.lastname: Zareian
authors.forename: Seyed-Omid
authors.initials: SO
authors.lastname: Ranaei-Siadat
authors.forename: Khosro
authors.initials: K
authors.lastname: Khajeh
mesh_terms: D000494:Allosteric Regulation; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D019757:Carbon-Oxygen Lyases / Q000737:chemistry* / Q000235:genetics; D020134:Catalytic Domain; D004795:Enzyme Stability; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D010710:Phosphates / Q000737:chemistry; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics; D013824:Thermus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D010710:Phosphates; D021122:Protein Subunits; D019757:Carbon-Oxygen Lyases; C021578:methylglyoxal synthase