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EC Number
General Information
Commentary
Reference
evolution
genetic environment of the mak gene in different organisms. Organization of the region containing the mak gene, overview
evolution
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview
metabolism
involvement of maltose-1-phosphate in the regulation of sugar metabolism in Escherichia coli
metabolism
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan
metabolism
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan; the enzyme PepS is involved in the cytoplasmic GlgE-pathway that converts trehalose to alpha(1->4),alpha(1->6)-linked glucan in 4 steps
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metabolism
the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose
metabolism
the enzyme PepS is involved in the cytoplasmic GlgE-pathway that converts trehalose to alpha(1->4),alpha(1->6)-linked glucan in 4 steps
more
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
more
the enzyme shows an eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases, a typical eukaryotic protein kinase-like fold. Subtle structural rearrangements occur upon nucleotide binding in the cleft between the N- and the C-terminal lobes. The enzyme has a phosphate-binding region in the N-terminal lobe that is proposed to act as an anchoring point tethering maltokinase and trehalose isomerase activities to the site of glycogen biosynthesis, ensuring correct regulation of Mak activity and possibly preventing excessive accumulation of maltose 1-phosphate. The enzyme's unusual N-terminal domain, with the 146AMLKV150 motif, containing the conserved phosphate-binding lysine residue, might regulate its phosphotransfer activity and represents the most likely anchoring point for TreS, the upstream enzyme in the pathway. Putative catalytic base is residue Asp305
physiological function
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate
Results 1 - 10 of 11 > >>