This enzyme belongs to the glycosidase family-13. Although this enzyme binds a calcium ion, it is distant from the active site and not involved in catalysis. According to the literature [10] & [22], this enzyme has a similar catalytic mechanism to that of alpha-amylase (D00165 in EzCatDB). Asp325 of 1bvz (PDB) acts as a nucleophile, whereas Glu354 acts as an acid-base. Asp421 probably stabilizes transition state. (1) Glu354 initiates the reaction by protonating O4 atom, giving an oxocarbonium ion-like transition state. (2) Asp325 makes a nucleophilic attack on the C1 atom to form glycosyl-enzyme intermediate. (3) Glu354 acts as a general base to activate a water. (4) The activated water attacks on the intermediate to complete the hydrolysis.
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
ASN 147;ASN 149; ;SER 153;GLY 172;ASP 174(Calcium binding)
Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages.
Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
A convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II).
alpha-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction.
Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability.
Structural consequences of neopullulanase mutations.
Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
Introducing transglycosylation activity in a liquefying alpha-amylase.
Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
Analysis of catalytic residues of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) by site-directed mutagenesis.
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.
Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins.
Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose.
Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.
Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution.
Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis.
Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase.
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.