2.7.1.175	evolution	genetic environment of the mak gene in different organisms. Organization of the region containing the mak gene, overview	717432	
2.7.1.175	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	-, 739666	
2.7.1.175	metabolism	involvement of maltose-1-phosphate in the regulation of sugar metabolism in Escherichia coli	717432	
2.7.1.175	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	-, 739666	
2.7.1.175	metabolism	the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose	-, 717816	
2.7.1.175	metabolism	the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2	-, 759499	
2.7.1.175	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	-, 737320	
2.7.1.175	additional information	enzyme complex structure analysis and location of active sites, overview	-, 759499	
2.7.1.175	additional information	stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview	-, 737320	
2.7.1.175	additional information	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	-, 739666