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

Martins, Rita LU ; Delgado, Osvaldo LU and Hatti-Kaul, Rajni LU (2003) In Biotechnology Letters 25(18). p.1555-1562
Abstract
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.... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology Letters
volume
25
issue
18
pages
1555 - 1562
publisher
Springer
external identifiers
  • wos:000184957400013
  • pmid:14571982
  • scopus:0141525436
ISSN
1573-6776
DOI
10.1023/A:1025430532333
language
English
LU publication?
yes
id
734596b8-60c5-4407-8afd-c3b3cac9804c (old id 129216)
date added to LUP
2007-07-02 13:41:38
date last changed
2018-01-07 08:47:05
@article{734596b8-60c5-4407-8afd-c3b3cac9804c,
  abstract     = {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.},
  author       = {Martins, Rita and Delgado, Osvaldo and Hatti-Kaul, Rajni},
  issn         = {1573-6776},
  language     = {eng},
  number       = {18},
  pages        = {1555--1562},
  publisher    = {Springer},
  series       = {Biotechnology Letters},
  title        = {Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens strain LS-3C.},
  url          = {http://dx.doi.org/10.1023/A:1025430532333},
  volume       = {25},
  year         = {2003},
}