title: Molecular genetic analysis of the pullulanase B gene of Bacillus acidopullulyticus.
abstract: A fragment from Bacillus acidopullulyticus strain 294-16 encoding a pullulanase activity has been cloned into Bacillus subtilis. The nucleotide sequence of the 3972 base pairs (bp) fragment has been determined and shown to include only one complete open reading frame (ORF) of 863 codons. The deduced amino acid sequence of this ORF, denoted pulB, shows homology to a number of amylolytic enzymes. Primary and secondary structure analysis indicates that the central region of the protein forms the catalytic domain in a characteristic (beta/alpha)8 barrel. Three carboxylic acid residues essential for catalysis were identified. Regions within the catalytic domain proposed to be involved in substrate binding have been identified by homology.
authors.affiliation: Genetics Department, Dublin University, Trinity College, Ireland.
authors.forename: A P
authors.initials: AP
authors.lastname: Kelly
authors.forename: B
authors.initials: B
authors.lastname: Diderichsen
authors.forename: S
authors.initials: S
authors.lastname: Jorgensen
authors.forename: D J
authors.initials: DJ
authors.lastname: McConnell
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D005798:Genes, Bacterial / Q000235:genetics*; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D006026:Glycoside Hydrolases; C100181:pullulanase