公开(公告)号：US06500659B1

公开(公告)日：2002-12-31

申请号：US09427372

申请日：1999-10-25

申请人： Dennis Murphy ,  John Reid ,  Dan Robertson

发明人： Dennis Murphy ,  John Reid ,  Dan Robertson

IPC分类号： C12N120

CPC分类号： C12P21/06 ,  C12N9/80

摘要： A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionally, a step which is very difficult to achieve with nonenzymatic methods.

摘要翻译： 纯化的热稳定性酶来源于弓形虫Thermococcus GU5L5。 该酶的分子量约为68.5千道尔顿，具有纤维素酶活性。 该酶可以由天然的或重组的宿主细胞产生，并且可用于从肽或肽模拟合成中的肽的N-末端去除精氨酸，苯丙氨酸或甲硫氨酸氨基酸。 该酶对于氨基酸衍生物的L或“天然”对映异构体是选择性的，因此可用于制备光学活性化合物。这些反应可以在化学上更有活性的酯的功能性存在下进行，其步骤是 用非酶法很难实现。