| Autor: |
Brizio C; Dipartimento di Biochimica e Biologia Molecolare E. Quagliariello, Università degli Studi di Bari, Via Orabona 4, 70126 Bari, Italy., Brandsch R, Douka M, Wait R, Barile M |
| Jazyk: |
angličtina |
| Zdroj: |
International journal of biological macromolecules [Int J Biol Macromol] 2008 Jun 01; Vol. 42 (5), pp. 455-62. Date of Electronic Publication: 2008 Mar 13. |
| DOI: |
10.1016/j.ijbiomac.2008.03.001 |
| Abstrakt: |
The precursor of the rat mitochondrial flavoenzyme dimethylglycine dehydrogenase (Me(2)GlyDH) has been produced in Escherichia coli as a C-terminally 6-His-tagged fusion protein, purified by one-step affinity chromatography and identified by ESI-MS/MS. It was correctly processed into its mature form upon incubation with solubilized rat liver mitoplasts. The purified precursor was mainly in its apo-form as demonstrated by immunological and fluorimetric detection of covalently bound flavin adenine dinucleotide (FAD). Results described here definitively demonstrate that: (i) covalent attachment of FAD to Me(2)GlyDH apoenzyme can proceed in vitro autocatalytically, without third reactants; (ii) the removal of mitochondrial presequence by mitochondrial processing peptidase is not required for covalent autoflavinylation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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