Characterization of genes from Thermoanaerobacterium thermosulfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains

被引:27
作者
Matuschek, M [1 ]
Sahm, K [1 ]
Zibat, A [1 ]
Bahl, H [1 ]
机构
[1] UNIV GOTTINGEN,INST MIKROBIOL,D-37077 GOTTINGEN,GERMANY
来源
MOLECULAR & GENERAL GENETICS | 1996年 / 252卷 / 04期
关键词
pullulanase; xylanase; polygalacturonate hydrolase; S-layer; thermophilic bacteria;
D O I
10.1007/BF02173016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two genes from Thermoanaerobacterium thermosulfurigenes EM1 were identified which are predicted to encode a xylanase (XynA) and a polygalacturonate hydrolase (PglA). The xynA gene has the potential to encode a 1234-amino acid product consisting of a signal peptide followed by a repeated domain, a xylanase family F domain, two cellulose-binding domains and a triplicated sequence at its C-terminus. The gene pglA is predicted to encode a product of 1148 amino acids consisting of a signal sequence followed by a fibronectin type III-like domain (Fn3 domain), the catalytic domain, a Gly/Thr/Ser/Asn-rich segment and a triplicated domain. The triplicated segments at the C-termini of deduced XynA and PglA are about 95% identical to each other and to the S-layer-like domains of the previously characterized pullulanase (AmyB) from the same organism. In contrast, sequence comparisons revealed only distant amino acid sequence similarities between the fibronectin type III-like domains of PglA and AmyB from T. thermosulfurigenes EM1.
引用
收藏
页码:493 / 496
页数:4
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