通过突变苯丙氨酸氨甲酰转移酶中的单个活性位点残基来工程化对映选择性的酪氨酸氨基转移酶。
Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase.
机构信息
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
出版信息
Chem Commun (Camb). 2010 Nov 21;46(43):8157-9. doi: 10.1039/c0cc02768e. Epub 2010 Oct 5.
By replacing a single active-site residue Cys107 with Ser in phenylalanine aminomutase (PAM), the enzyme gained tyrosine aminomutase (TAM) activity while retaining PAM activity and high enantioselectivity. This engineered enantioselective TAM also catalyzed formation of β-tyrosine from p-coumaric acid and may prove to be useful for the synthesis of enantiopure β-tyrosine and its derivatives.
通过将苯丙氨酸氨甲酰基转移酶（PAM）中的一个活性位点残基半胱氨酸 107 替换为丝氨酸，该酶获得了酪氨酸氨甲酰基转移酶（TAM）活性，同时保留了 PAM 活性和高对映选择性。这种工程化的对映选择性 TAM 还可以催化对羟基肉桂酸生成β-酪氨酸，这可能对合成对映纯β-酪氨酸及其衍生物有用。
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