酪氨酸
酶
生物化学
化学
苯丙氨酸
生物催化
生物合成
立体化学
苯丙氨酸解氨酶
氨基酸
催化作用
反应机理
作者
Yannik Brack,Chenghai Sun,Dong Yi,Uwe T. Bornscheuer
出处
期刊:ChemBioChem
[Wiley]
日期:2022-04-07
卷期号:23 (10)
被引量:10
标识
DOI:10.1002/cbic.202200062
摘要
Abstract p ‐Coumaric acid ( p ‐CA) is a key precursor for the biosynthesis of flavonoids. Tyrosine ammonia lyases (TALs) specifically catalyze the synthesis of p ‐CA from l ‐tyrosine, which is a convenient enzymatic pathway. To explore novel and highly active TALs, a phylogenetic tree‐building approach was conducted including 875 putative TALs and 46 putative phenylalanine/tyrosine ammonia lyases (PTALs). Among them, 5 TALs and 3 PTALs were successfully characterized and found to exhibit the proposed enzymatic activity. The TAL from Chryseobacterium luteum sp. nov (TAL clu ) has the highest affinity ( K m =0.019 m m ) and conversion efficiency ( k cat / K m= 1631 s −1 ⋅ m m −1 ) towards l ‐tyrosine. The reaction conditions for two purified enzymes and their E. coli recombinant cells were optimized and p ‐CA yields of 2.03 g/L after 8 hours by TAL clu and 2.35 g/L after 24 h by TAL from Rivularia sp. PCC 7116 (TAL rpc ) in whole cells were achieved. These TALs are thus candidates for the construction of whole‐cell systems to produce the flavonoid precursor p ‐CA.
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