Construction of minimum size cellulase (Cel5Z) from Pectobacterium chrysanthemi PY35 by removal of the C-terminal region |
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Authors: | Woo Jin Lim Su Young Hong Chang Long An Kye Man Cho Byoung Rock Choi Young Kyun Kim Jin Mee An Jung Mi Kang Sun Mi Lee Soo Jeong Cho Hoon Kim Han Dae Yun |
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Institution: | (1) Division of Applied Life Science, Gyeongsang National University, Chinju, 660-701, Korea;(2) Research Institute of Life Science, Gyeongsang National University, Chinju, 660-701, Korea;(3) Department of Agricultural Chemistry, Sunchon National University, Sunchon, 540-742, Korea |
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Abstract: | Pectobacterium chrysanthemi PY35 secretes the endoglucanase Cel5Z, an enzyme of the glycoside hydrolase family 5. Cel5Z is a 426 amino acid, signal peptide (SP)-containing protein composed of two domains: a large N-terminal catalytic domain (CD; 291 amino acids) and a small C-terminal cellulose binding domain (CBD; 62 amino acids). These two domains are separated by a 30 amino acid linker region (LR). A truncated cel5Z gene was constructed with the addition of a nonsense mutation that removes the C-terminal region of the protein. A truncated Cel5Z protein, consisting of 280 amino acid residues, functioned as a mature enzyme despite the absence of the SP, 11 amino acid CD, LR, and CBD region. In fact, this truncated Cel5Z protein showed an enzymatic activity 80% higher than that of full-length Cel5Z. However, cellulase activity was undetectable in mature Cel5Z proteins truncated to less than 280 amino acids. |
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