An exo-type maltose-forming alpha-amylase alpha-1,4- and alpha-1,6-glucan hydrolytic activity. It acts on the non-reducing end of the substrate and requires at least a G2 unit at its working site
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
An exo-type maltose-forming alpha-amylase alpha-1,4- and alpha-1,6-glucan hydrolytic activity. It acts on the non-reducing end of the substrate and requires at least a G2 unit at its working site
at an early stage of the reaction only maltose and 4-nitrophenol alpha-D-maltotetraoside, but not maltotetraose are observed. Even as the reaction proceeded, maltotetraose does not appear at all
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a maltose unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off maltose unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points. 6-O-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant to hydrolysis
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Substrate specificity and binding, docking modelling, overview
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Substrate specificity and binding, docking modelling, overview
pH 4.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin
the enzyme structure shows a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles. The catalytic residues are Glu153 and Asp253 at the domain interface
the enzyme structure shows a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles. The catalytic residues are Glu153 and Asp253 at the domain interface
2 * 70191, recombinant enzyme, SDS-PAGE, in the dimeric structure, extensive interactions including Asn185-Gly327, Glu224-Lys241 and Gly327-Asn185 hydrogen bonds and a Glu224-Lys241 salt bridge between two (beta/alpha)7-barrels of the N-domains comprise the dimer associations
2 * 70191, recombinant enzyme, SDS-PAGE, in the dimeric structure, extensive interactions including Asn185-Gly327, Glu224-Lys241 and Gly327-Asn185 hydrogen bonds and a Glu224-Lys241 salt bridge between two (beta/alpha)7-barrels of the N-domains comprise the dimer associations
2 * 70191, recombinant enzyme, SDS-PAGE, in the dimeric structure, extensive interactions including Asn185-Gly327, Glu224-Lys241 and Gly327-Asn185 hydrogen bonds and a Glu224-Lys241 salt bridge between two (beta/alpha)7-barrels of the N-domains comprise the dimer associations
the enzyme structure shows a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles, two domains assemble to form a groove in the active site
the enzyme structure shows a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles, two domains assemble to form a groove in the active site
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled wild-type enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 15 mg/ml protein solution with 0.001 ml of reservoir solution consisting of 1.0 M ammonium citrate dibasic, 0.8 M sodium acetate trihydrate pH 4.6, 18°C, X-ray diffraction structure determination and analysis at 1..8 A resolution
Jeon, E.J.; Jung, J.H.; Seo, D.H.; Jung, D.H.; Holden, J.F.; Park, C.S.
Bioinformatic and biochemical analysis of a novel maltose-forming alpha-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1