Sequence analysis of Cyclodextrin Glycosyltransferase from the alkaliphilic Bacillus agaradhaerens strain LS-3C.

MARTINS R; DELGADO O D; HATTI-KAUL R

BIOTECHNOLOGY LETTERS

Springer

Lugar: Londres; Año: 2003 vol. 25 p. 1555 - 1562

0141-5492

The gene encoding an alkaline active cyclodextrin glycosyltransferase (CGTase) from the alkaliphilic B. agaradhaerens LS-3C was cloned and sequenced. It encodes a mature polypeptide of 679 amino acids with a molecular mass of 76 488 Da. The deduced amino acid sequence of the mature CGTase revealed 99 and 95% identity to the CGTase sequences from the other B. agaradhaerens strains, DSM 8721T and 9948, respectively. The next closest identity was of 59% with B. clarkii enzyme. CGTases from B. agaradhaerens, B. clarkii, and B. firmus/lentus formed a phylogenetically separated cluster from the other CGTases of Bacillus spp. origin. A number of usually conserved residues in the CGTases were found to be replaced in the sequence of B. agaradhaerens enzyme. The sequence analysis indicated the enzyme to be close to the so-called ‘intermediary enzymes’ in the α-amylase family.