Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens strain LS-3C.

Research output: Contribution to journalArticle

Standard

Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens strain LS-3C. / Martins, Rita; Delgado, Osvaldo; Hatti-Kaul, Rajni.

In: Biotechnology Letters, Vol. 25, No. 18, 2003, p. 1555-1562.

Research output: Contribution to journalArticle

Harvard

APA

CBE

MLA

Vancouver

Author

RIS

TY - JOUR

T1 - Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens strain LS-3C.

AU - Martins, Rita

AU - Delgado, Osvaldo

AU - Hatti-Kaul, Rajni

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

U2 - 10.1023/A:1025430532333

DO - 10.1023/A:1025430532333

M3 - Article

VL - 25

SP - 1555

EP - 1562

JO - Biotechnology Letters

T2 - Biotechnology Letters

JF - Biotechnology Letters

SN - 1573-6776

IS - 18

ER -