scholarly journals Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli.

1993 ◽  
Vol 268 (32) ◽  
pp. 24402-24407
Author(s):  
K.A. Laderman ◽  
K Asada ◽  
T Uemori ◽  
H Mukai ◽  
Y Taguchi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pyrococcus Furiosus ◽  
Alpha Amylase ◽  
Cloning And Sequencing ◽  
Expression In Escherichia Coli

Cloning and sequencing of a gene from the archaeon Pyrococcus furiosus with high homology to a gene encoding phosphoenolpyruvate synthetase from Escherichia coli

Gene ◽  
1995 ◽  
Vol 160 (1) ◽  
pp. 101-103 ◽  
Author(s):  
Carol E. Jones ◽  
Toni M. Fleming ◽  
Peter W. Piper ◽  
Jennifer A. Littlechild ◽  
Don A. Cowan
Keyword(s):  
Escherichia Coli ◽  
Pyrococcus Furiosus ◽  
High Homology ◽  
Cloning And Sequencing ◽  
Gene Encoding

scholarly journals Cloning and Sequencing of a Poly(dl-Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

2003 ◽  
Vol 69 (5) ◽  
pp. 2498-2504 ◽  
Author(s):  
Yukie Akutsu-Shigeno ◽  
Teerawat Teeraphatpornchai ◽  
Kamonluck Teamtisong ◽  
Nobuhiko Nomura ◽  
Hiroo Uchiyama ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactic Acid ◽  
Amino Acid ◽  
Functional Expression ◽  
Amino Acid Residues ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
Butylene Succinate ◽  
Expression In Escherichia Coli ◽  
Poly Ethylene

ABSTRACT The gene encoding a poly(dl-lactic acid) (PLA) depolymerase from Paenibacillus amylolyticus strain TB-13 was cloned and overexpressed in Escherichia coli. The purified recombinant PLA depolymerase, PlaA, exhibited degradation activities toward various biodegradable polyesters, such as poly(butylene succinate), poly(butylene succinate-co-adipate), poly(ethylene succinate), and poly(ε-caprolactone), as well as PLA. The monomeric lactic acid was detected as the degradation product of PLA. The substrate specificity toward triglycerides and p-nitrophenyl esters indicated that PlaA is a type of lipase. The gene encoded 201 amino acid residues, including the conserved pentapeptide Ala-His-Ser-Met-Gly, present in the lipases of mesophilic Bacillus species. The identity of the amino acid sequence of PlaA with Bacillus lipases was no more than 45 to 50%, and some of its properties were different from those of these lipases.

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