Open AccessMolecular genetic analysis of the pullalanase B gene of Bacillus acidopullulyticus
Author(s) -
Kelly Adrian P.,
Diderichsen Borge,
Jorgensen Steen,
McConnell David J.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06621.x
Subject(s) - bacillus subtilis , open reading frame , homology (biology) , nucleic acid sequence , gene , genetics , biology , peptide sequence , chemistry , stereochemistry , bacteria
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.