| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235584 | Process Biochemistry | 2012 | 8 Pages |
Abstract
⺠We characterize a β-glucosidase (NfBGL1) from Neosartorya fischeri. ⺠NfBGL1 is distinguished from other BGLs by its high turnover rate. ⺠E445 in NfBGL1 is identified as an important residue affecting its substrate affinity. ⺠An acidic amino acid at position 445 is a determinant for the substrate binding of BGLs.
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Authors
Manish Kumar Tiwari, Kyoung-Mi Lee, Dayanand Kalyani, Raushan Kumar Singh, Hoon Kim, Jung-Kul Lee, Priyadharshini Ramachandran,