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Molecular genetic analysis of the pullalanase B gene of Bacillus acidopullulyticus

Adrian P. Kelly , Borge Diderichsen , Steen Jorgensen , David J. McConnell
DOI: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06621.x 97-105 First published online: 1 January 1994


A fragment from Bacillus acidopullulyticus strain 294-16 encoding a pullunase 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 characteristics (β/α)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.

Key words
  • Pullulanase
  • Bacillus acidopullulyticus

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