5jy7 | pdb_00005jy7
From Proteopedia
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Complex of Mycobacterium smegmatis trehalose synthase with maltokinase
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Structural highlights
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Function[TRES_MYCS2] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.[1] [2] [3] [4] [MAK_MYCS2] Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate (Probable). Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB.[5] References
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This page was last modified 13:44, 24 May 2017.