Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus

Greg D. Albertson; Ronald H. McHale; Moreland D. Gibbs; Peter L. Bergquist

doi:10.1016/S0167-4781(97)00123-1

Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus

Greg D. Albertson, Ronald H. McHale, Moreland D. Gibbs, Peter L. Bergquist^*

^*Corresponding author for this work

Macquarie University Administration Unit

Research output: Contribution to journal › Article › peer-review

37 Citations (Scopus)

Abstract

A gene coding for a pullulanase from the obligately anaerobic, extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus has been cloned in Escherichia coli. It consists of an open reading frame (pulA) of 2478 bp which codes for an enzyme of 95 732 Da and is flanked by two other open reading frames. A truncated version of the gene which lacks 381 bp of 5'- sequence also has pullulanase activity and it appears that the amino-terminal portion of the gene is not essential for either activity or thermostability. Amino acid sequence comparisons with other published amylases and pullulanases showed that it possesses homology to the four key regions common to these enzymes.

Original language	English
Pages (from-to)	35-39
Number of pages	5
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1354
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4781(97)00123-1
Publication status	Published - Oct 1997

Keywords

Amino acid motif
Amylopullulanase
Gene cloning
Thermophile
Type I pullulanase

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10.1016/S0167-4781(97)00123-1

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title = "Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus",

abstract = "A gene coding for a pullulanase from the obligately anaerobic, extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus has been cloned in Escherichia coli. It consists of an open reading frame (pulA) of 2478 bp which codes for an enzyme of 95 732 Da and is flanked by two other open reading frames. A truncated version of the gene which lacks 381 bp of 5'- sequence also has pullulanase activity and it appears that the amino-terminal portion of the gene is not essential for either activity or thermostability. Amino acid sequence comparisons with other published amylases and pullulanases showed that it possesses homology to the four key regions common to these enzymes.",

keywords = "Amino acid motif, Amylopullulanase, Gene cloning, Thermophile, Type I pullulanase",

author = "Albertson, {Greg D.} and McHale, {Ronald H.} and Gibbs, {Moreland D.} and Bergquist, {Peter L.}",

year = "1997",

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doi = "10.1016/S0167-4781(97)00123-1",

language = "English",

volume = "1354",

pages = "35--39",

journal = "BBA - Gene Structure and Expression",

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publisher = "Elsevier",

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}

Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus. / Albertson, Greg D.; McHale, Ronald H.; Gibbs, Moreland D. et al.

In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1354, No. 1, 10.1997, p. 35-39.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus

AU - Albertson, Greg D.

AU - McHale, Ronald H.

AU - Gibbs, Moreland D.

AU - Bergquist, Peter L.

PY - 1997/10

Y1 - 1997/10

N2 - A gene coding for a pullulanase from the obligately anaerobic, extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus has been cloned in Escherichia coli. It consists of an open reading frame (pulA) of 2478 bp which codes for an enzyme of 95 732 Da and is flanked by two other open reading frames. A truncated version of the gene which lacks 381 bp of 5'- sequence also has pullulanase activity and it appears that the amino-terminal portion of the gene is not essential for either activity or thermostability. Amino acid sequence comparisons with other published amylases and pullulanases showed that it possesses homology to the four key regions common to these enzymes.

AB - A gene coding for a pullulanase from the obligately anaerobic, extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus has been cloned in Escherichia coli. It consists of an open reading frame (pulA) of 2478 bp which codes for an enzyme of 95 732 Da and is flanked by two other open reading frames. A truncated version of the gene which lacks 381 bp of 5'- sequence also has pullulanase activity and it appears that the amino-terminal portion of the gene is not essential for either activity or thermostability. Amino acid sequence comparisons with other published amylases and pullulanases showed that it possesses homology to the four key regions common to these enzymes.

KW - Amino acid motif

KW - Amylopullulanase

KW - Gene cloning

KW - Thermophile

KW - Type I pullulanase

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JO - BBA - Gene Structure and Expression

JF - BBA - Gene Structure and Expression

SN - 0167-4781

IS - 1

ER -

Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus

Abstract

Keywords

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