| Autor: |
Fujita, Akihiro, Kawashima, Akira, Noguchi, Yuji, Hirose, Shuichi, Kitagawa, Noriaki, Watanabe, Hikaru, Mori, Tetsuya, Nishimoto, Tomoyuki, Aga, Hajime, Ushio, Shimpei, Yamamoto, Koryu |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2022, Vol. 86 Issue: 1 p68-77, 10p |
| Abstrakt: |
We performed whole genome sequence analyses of Agreiasp. D1110 and Microbacterium trichothecenolyticumD2006 that secrete enzymes to produce cyclo-{→6)-α-d-Glcp-(1→6)-α-d-Glcp-(1→6)-α-d-Glcp-(1→6)-α-d-Glcp-(1→} (CI4) from dextran. Full-length amino acid sequences of CI4-forming enzymes were identified by matching known N-terminal amino acid sequences with products of the draft genome. Domain searches revealed that the CI4-forming enzymes are composed of Glycoside Hydrolase family 66 (GH66) domain, Carbohydrate Binding Module family 35 (CBM35) domain, and CBM13 domain, categorizing the CI4-forming enzymes in the GH66. Furthermore, the amino acid sequences of the two CI4-forming enzymes were 71% similar to each other and up to 51% similar to cycloisomaltooligosaccharide glucanotransferases (CITases) categorized in GH66. Differences in sequence between the CI4-forming enzymes and the CITases suggest mechanisms to produce specific cycloisomaltooligosaccharides, and whole genome sequence analyses identified a gene cluster whose gene products likely work in concert with the CI4-forming enzymes.Graphical AbstractModel of CI4-production and CI4-metabolism in CI4-producing bacteria. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
