Linder M, Lindeberg G, Reinikainen T, Teeri T T, Pettersson G
VTT Biotechnology and Food Research, Espoo, Finland.
FEBS Lett. 1995 Sep 18;372(1):96-8. doi: 10.1016/0014-5793(95)00961-8.
Cellulose-binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose-binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose-binding face.
纤维素结合结构域（CBDs）构成了大多数纤维素分解酶的独特功能单元。我们比较了里氏木霉的纤维二糖水解酶I（CBHI）和内切葡聚糖酶I（EGI）的CBDs与纤维素的结合亲和力。EGI的CBD比CBHI的CBD具有显著更高的亲和力。为了确定导致EGI中亲和力增加的残基，制备了CBHI CBD的四种变体。大部分差异可归因于在平坦的纤维素结合面上酪氨酸被色氨酸取代。
