Mitra A, Kitamura Y, Gasson M J, Narbad A, Parr A J, Payne J, Rhodes M J, Sewter C, Walton N J
Institute of Food Research-Norwich Laboratory, Norwich Research Park, Norwich, Colney, NR4 7UA, United Kingdom.
Arch Biochem Biophys. 1999 May 1;365(1):10-6. doi: 10.1006/abbi.1999.1140.
The enzyme 4-hydroxycinnamoyl-CoA hydratase/lyase (HCHL), which catalyzes a hydration and two-carbon cleavage step in the degradation of 4-hydroxycinnamic acids, has been purified and characterized from Pseudomonas fluorescens strain AN103. The enzyme is a homodimer and is active with three closely related substrates, 4-coumaroyl-CoA, caffeoyl-CoA, and feruloyl-CoA (Km values: 5.2, 1.6, and 2.4 microM, respectively), but not with cinnamoyl-CoA or with sinapinoyl-CoA. The abundance of the enzyme reflects a low catalytic center activity (2.3 molecules s-1 at 30 degrees C; 4-coumaroyl-CoA as substrate).
已从荧光假单胞菌菌株AN103中纯化并鉴定出4-羟基肉桂酰辅酶A水合酶/裂解酶(HCHL),该酶在4-羟基肉桂酸降解过程中催化水合和二碳裂解步骤。该酶是一种同型二聚体,对三种密切相关的底物4-香豆酰辅酶A、咖啡酰辅酶A和阿魏酰辅酶A有活性(Km值分别为5.2、1.6和2.4 microM),但对肉桂酰辅酶A或芥子酰辅酶A无活性。该酶的丰度反映出其催化中心活性较低(30℃时为2.3分子·秒-1;以4-香豆酰辅酶A为底物)。