一种来自洋葱伯克霍尔德菌的新型依赖于Fe(II)/α-酮戊二酸的双加氧酶具有N-琥珀酰-L-亮氨酸的β-羟基化活性。
A novel Fe(II)/α-ketoglutarate-dependent dioxygenase from Burkholderia ambifaria has β-hydroxylating activity of N-succinyl l-leucine.
作者信息
Hibi M, Kawashima T, Kasahara T, Sokolov P M, Smirnov S V, Kodera T, Sugiyama M, Shimizu S, Yokozeki K, Ogawa J
机构信息
Industrial Microbiology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan Ajinomoto-Genetika Research Institute, Moscow, Russia Institute of Food Sciences & Technologies Food Product Division, Ajinomoto Co., Inc., Kawasaki, Japan Research Institute for Bioscience Products & Fine Chemicals, Ajinomoto Co., Inc., Kawasaki, Japan.
出版信息
Lett Appl Microbiol. 2012 Dec;55(6):414-9. doi: 10.1111/j.1472-765X.2012.03308.x. Epub 2012 Oct 8.
An Fe(II)/α-ketoglutarate-dependent dioxygenase, SadA, was obtained from Burkholderia ambifaria AMMD and heterologously expressed in Escherichia coli. Purified recombinant SadA had catalytic activity towards several N-substituted l-amino acids, which was especially strong with N-succinyl l-leucine. With the NMR and LC-MS analysis, SadA converted N-succinyl l-leucine into N-succinyl l-threo-β-hydroxyleucine with >99% diastereoselectivity. SadA is the first enzyme catalysing β-hydroxylation of aliphatic amino acid-related substances and a potent biocatalyst for the preparation of optically active β-hydroxy amino acids.
一种依赖Fe(II)/α-酮戊二酸的双加氧酶SadA，是从洋葱伯克霍尔德菌AMMD中获得的，并在大肠杆菌中进行了异源表达。纯化后的重组SadA对几种N-取代的L-氨基酸具有催化活性，对N-琥珀酰-L-亮氨酸的催化活性尤为强烈。通过核磁共振（NMR）和液相色谱-质谱（LC-MS）分析，SadA将N-琥珀酰-L-亮氨酸转化为N-琥珀酰-L-苏式-β-羟基亮氨酸，非对映选择性大于99%。SadA是第一种催化脂肪族氨基酸相关物质β-羟基化的酶，也是制备光学活性β-羟基氨基酸的高效生物催化剂。
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