Cloning and characterization of a novel tyrosine ammonia lyase-encoding gene involved in bagremycins biosynthesis in Streptomyces sp
Tyrosine ammonia lyase catalyzes the deamination of L-tyrosine to trans-coumaric acid. A novel tyrosine ammonia lyase-encoding gene, bagA, was cloned and sequenced from bagremycins-producing strain Streptomyces sp. Tü 4128 whose protein product contains a Ala–Ser–Gly segment in the active site. The...
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Veröffentlicht in: | Biotechnology letters 2012-02, Vol.34 (2), p.269-274 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Tyrosine ammonia lyase catalyzes the deamination of L-tyrosine to trans-coumaric acid. A novel tyrosine ammonia lyase-encoding gene, bagA, was cloned and sequenced from bagremycins-producing strain Streptomyces sp. Tü 4128 whose protein product contains a Ala–Ser–Gly segment in the active site. The disruption of the bagA gene abolished trans-coumaric acid and bagremycins production. trans-coumaric acid restored the formation of bagremycin A in the mutant, but not bagremycin B. Thus, trans-coumaric acid is a precursor for biosynthesis of bagremycins and the bagA gene codes for tyrosine ammonia lyase to synthesize trans-coumaric acid. This is a novel bacterial tal gene reported in actinomycetes for the second time and for the first time in a Streptomyces sp. |
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ISSN: | 0141-5492 1573-6776 |
DOI: | 10.1007/s10529-011-0755-9 |