| Autor: |
K A Sment, J Konisky, A A DiMarco, R. S. Wolfe |
| Rok vydání: |
1990 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 265:472-476 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(19)40254-8 |
| Popis: |
The formylmethanofuran:tetrahydromethanopterin formyltransferase (FTR) from Methanobacterium thermoautotrophicum delta H was cloned and its sequence was determined. The clone was contained on a 4.8-kilobase BamHI fragment of M. thermoautotrophicum DNA ligated into pBR329. When this fragment was subcloned into the phagemid pTZ18R, a functional enzyme was synthesized under control of the lac promoter. Sequence analysis revealed the presence of a ribosome binding site and a possible terminator structure. The absence of an identifiable promoter lends credibility to the open reading frame which is present 5' to ftr. The ftr gene encodes an acidic protein with a calculated molecular weight of 31,401. The sequence of FTR does not appear to be homologous to any other sequenced proteins, including proteins which use pterin substrates. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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