title: Enzymatic synthesis of c-di-GMP using inclusion bodies of Thermotoga maritima full-length diguanylate cyclase.
abstract: Recombinant full-length diguanylate cyclases (DGCs) of Thermotoga maritima with native and mutant allosteric sites were overexpressed in Escherichia coli cells and characterized. It has been shown that target enzymes are produced substantially in the form of active inclusion bodies. Introduction of the mutation in allosteric site resulted in 7-fold increase of the T. maritima DGC activity. Possibility of applying full-length DGC of T. maritima in the form of inclusion bodies for synthesis of c-di-GMP was originally demonstrated.
authors.affiliation: Institute of Microbiology, National Academy of Sciences, Minsk, Belarus.
authors.forename: A S
authors.initials: AS
authors.lastname: Korovashkina
authors.forename: A N
authors.initials: AN
authors.lastname: Rymko
authors.forename: S V
authors.initials: SV
authors.lastname: Kvach
authors.forename: A  I
authors.initials: A
authors.lastname: Zinchenko
mesh_terms: D000495:Allosteric Site; D001709:Biotechnology; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000032:analysis / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D002479:Inclusion Bodies / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D019761:Phosphorus-Oxygen Lyases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012492:Salts; D020124:Thermotoga maritima / Q000201:enzymology*
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012492:Salts; C062025:bis(3',5')-cyclic diguanylic acid; D019761:Phosphorus-Oxygen Lyases; C060720:diguanylate cyclase; D006152:Cyclic GMP