The Type II Pullulanase of Thermococcus hydrothermalis: Molecular Characterization of the Gene and Expression of the Catalytic Domain
1999 ◽
Vol 181
(10)
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pp. 3284-3287
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Keyword(s):
Type Ii
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ABSTRACT The gene encoding a hyperthermostable type II pullulanase produced by Thermococcus hydrothermalis (Th-Apu) has been isolated. Analysis of a total of 5.2 kb of genomic DNA has revealed the presence of three open reading frames, one of which (apuA) encodes the pullulanase. This enzyme is composed of 1,339 amino acid residues and exhibits a multidomain structure. In addition to a typical N-terminal signal peptide, Th-Apu possesses a catalytic domain, a domain bearing S-layer homology-like motifs, a Thr-rich region, and a potential C-terminal transmembrane domain. The presence of these noncatalytic domains suggests that Th-Apu may be anchored to the cell surface and be O glycosylated.
2002 ◽
Vol 184
(1)
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pp. 216-223
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Keyword(s):
2005 ◽
Vol 187
(11)
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pp. 3889-3893
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2002 ◽
Vol 70
(11)
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pp. 5955-5964
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2007 ◽
Vol 73
(9)
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pp. 2769-2776
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2011 ◽
Vol 24
(7)
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pp. 827-838
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1994 ◽
Vol 68
(12)
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pp. 8239-8253
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