THE CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE-A (CENA) FROM CELLULOMONAS-FIMI - EVIDENCE FOR THE INVOLVEMENT OF TRYPTOPHAN RESIDUES IN BINDING
THE CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE-A (CENA) FROM CELLULOMONAS-FIMI - EVIDENCE FOR THE INVOLVEMENT OF TRYPTOPHAN RESIDUES IN BINDING
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DOI：
10.1111/j.1365-2958.1994.tb00352.x
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发表时间：
1994-02-01
影响因子：
3.6
通讯作者：
KILBURN, DG
中科院分区：
文献类型：
--
作者：
DIN, N;FORSYTHE, IJ;KILBURN, DG
纤维素单胞菌fimi内切-β-1-4-葡聚糖酶A（CenA）含有离散的N-末端纤维素结合结构域（CBDCenA）。相关的CBD存在于至少16种细菌聚糖酶中，其特征在于四个高度保守的Trp残基，其中两个对应于CBDCenA的W14和W 68。将CBDCenA对结晶纤维素的吸附与两种Trp突变体（W14 A和W 68 A）的吸附进行比较。突变体CBD对纤维素的亲和力相对于野生型分别降低了约50倍和30倍。物理测量表明，突变CBD折叠正常。荧光数据表明W14和W 68暴露在CBD上，这与它们参与与纤维素表面上的纤维二糖残基结合一致。
Cellulomonas fimi endo-beta-1-4-glucanase A (CenA) contains a discrete N-terminal cellulose-binding domain (CBDCenA). Related CBDs occur in at least 16 bacterial glycanases and are characterized by four highly conserved Trp residues, two of which correspond to W14 and W68 of CBDCenA. The adsorption of CBDCenA to crystalline cellulose was compared with that of two Trp mutants (W14A and W68A). The affinities of the mutant CBDs for cellulose were reduced by approximately 50- and 30-fold, respectively, relative to the wild type. Physical measurements indicated that the mutant CBDs fold normally. Fluorescence data indicated that W14 and W68 were exposed on the CBD, consistent with their participation in binding to cellobiosyl residues on the cellulose surface.