| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537178 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 7 Pages |
Abstract
⺠PFTA is a unique hyperthermophilic amylase with cyclodextrin hydrolysis activity. ⺠The crystal structure of PFTA shows that the enzyme is a self-sufficient monomer. ⺠The extended N-terminal region folded into its own active site. ⺠Mutant at the domain interface produced higher purity of maltoheptaose. ⺠Result supports functional substitution of the Nâ²âdomain in hyperthermophilic archaea.
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Authors
Jong-Tae Park, Hyung-Nam Song, Tae-Yang Jung, Myoung-Hee Lee, Sung-Goo Park, Eui-Jeon Woo, Kwan-Hwa Park,