Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters
Biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes...
Prif Awduron: | Wang, M, Moynié, L, Harrison, P, Kelly, V, Piper, A, Naismith, J, Campopiano, D |
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Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
Springer Nature
2017
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Eitemau Tebyg
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Cyhoeddwyd: (1984-02-01) -
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gan: J Roitelman, et al.
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