hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains
Synonyms
cyclodextrinase, MAase, maltogenic amylase, MalZ, More, SMMA, TMG, YvdF, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains
hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the reducing ends of the chains
MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6
MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6
MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4
SMMA hydrolyzes linear maltooligosaccharides, starch, cyclodextrins, and cycloamylose, primarily to maltose and glucose, and shows highest activity toward acarbose and pullulan, hydrolyzed to acarviosine-glucose and panose, respectively. Product analysis, overview
TMG is an exo-acting glucosidase possessing the characteristics of both CD-/pullulan hydrolyzing enzyme and alpha-glucosidase. It hydrolyzes various maltodextrins including maltotriose to maltoheptaose and cyclomaltodextrins to mainly glucose and maltose, but it cannot hydrolyze pullulan, but acarbose
the enzyme specifically cleaves a glucose unit from the reducing end of maltooligosaccharides unlike to other glucosidases. Since its enzymatic activity is negligible if alpha-methylglucoside is present in the reducing end, the type of the residue at the reducing end of the substrate is important for the TMG activity. It hydrolyzes various maltodextrins including maltotriose to maltoheptaose and cyclomaltodextrins to mainly glucose and maltose, but it cannot hydrolyze pullulan, but acarbose
TMG is an exo-acting glucosidase possessing the characteristics of both CD-/pullulan hydrolyzing enzyme and alpha-glucosidase. It hydrolyzes various maltodextrins including maltotriose to maltoheptaose and cyclomaltodextrins to mainly glucose and maltose, but it cannot hydrolyze pullulan, but acarbose
in SMMA, non-polar side chains at 357W, 408W, 449Y, 451W, 463Y, 490Y, 501Y, 517Y 519Y, 529Y, 593W, and 608Y are located at the termini of alpha-helixes and beta-sheets contributing to the extreme thermostability of the enzyme
construction of a malZ-yvdF fusion enzyme, MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4. Construction of yvdF, amyX, and yvdF amyX mutant strains, amyX encodes the a debranching enzyme pullulanase. The yvdF mutant exhibits limited degradation of the substrates beta-cyclodextrin and maltoheptaose, oligosaccharides spectrum, overview
construction of a malZ-yvdF fusion enzyme, MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4. Construction of yvdF, amyX, and yvdF amyX mutant strains, amyX encodes the a debranching enzyme pullulanase. The yvdF mutant exhibits limited degradation of the substrates beta-cyclodextrin and maltoheptaose, oligosaccharides spectrum, overview
in SMMA, non-polar side chains at 357W, 408W, 449Y, 451W, 463Y, 490Y, 501Y, 517Y 519Y, 529Y, 593W, and 608Y are located at the termini of alpha-helixes and beta-sheets contributing to the extreme thermostability of the enzyme
Lee, M.; Kim, Y.-W.; Kim, T.-J.; Park, C.-S.; Kim, J.-W.; Moon, T.-W.; Park, K.-H.
A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates
Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.
Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus