title: Molecular cloning and characterization of an alpha-amylase from Pichia burtonii 15-1.
abstract: An alpha-amylase secreted by Pichia burtonii 15-1 isolated from a traditional starter murcha of Nepal, named Pichia burtonii alpha-amylase (PBA), was studied. The gene was cloned and its nucleotide sequence was determined. PBA was deduced to consist of 494 amino acid residues. It shared certain degrees of amino acid sequence identity with other homologous proteins: 60% with Schwanniomyces occidentalis alpha-amylase, 58% with Saccharomycopsis sp. alpha-amylase, and 47% with Taka-amylase A from Aspergillus oryzae. A three-dimensional structural model of PBA generated using the known three-dimensional structure of Taka-amylase A as a template suggested high structural similarity between them. Kinetic analysis revealed that the K(m) values of PBA were lower than those of Taka-amylase A for the oligosaccharides. Although the k(cat) values of PBA were lower than those of Taka-amylase A for the oligosaccharide substrates, the k(cat)/K(m) values of PBA were higher.
authors: Department of Nutritional Science, Faculty of Applied Bio-Science, Tokyo University of Agriculture, Setagaya-ku, Tokyo, Japan.
authors: Saemi
authors: S
authors: Kato
authors: Akiko
authors: A
authors: Shimizu-Ibuka
authors: Kiyoshi
authors: K
authors: Mura
authors: Akiko
authors: A
authors: Takeuchi
authors: Chiyoko
authors: C
authors: Tokue
authors: Soichi
authors: S
authors: Arai
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010843:Pichia / Q000201:enzymology*; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D005656:Fungal Proteins; D000516:alpha-Amylases