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The N‐Terminal Domain of the Pullulanase from Anoxybacillus sp. WB42 Modulates Enzyme Specificity and Thermostability
ChemBioChem ( IF 3.2 ) Pub Date : 2018-04-14 , DOI: 10.1002/cbic.201700665
Jianfeng Wang 1, 2 , Zhongmei Liu 1 , Zhemin Zhou 1
Affiliation  

Enzyme engineering: The N‐terminal domain of the amylopullulanase PulWB42 is identified as carbohydrate‐binding module 68, in which residue 90 or 93 acts as a trigger to convert amylopullulanase into type I pullulanase, and the His5–Arg6–Thr7 segment or Gln87 impacts enzyme thermostability.
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中文翻译:

Anoxybacillus sp。的支链淀粉酶的N末端结构域。WB42调节酶特异性和热稳定性

酶工程:淀粉葡聚糖酶PulWB42的N末端结构域被确定为碳水化合物结合模块68,其中残基90或93触发将淀粉葡聚糖酶转化为I型支链淀粉酶,并且His5-Arg6-Thr7节段或Gln87影响酶热稳定性。
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更新日期:2018-04-14
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