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Structures of the cloned chitinase and its truncant from A-caviae

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Structures of the cloned chitinase and its truncant from A-caviae.htm (455bytes)
Date
2002
Author
Zhou, Y
周樱
Wang, FP
Xiao, X
肖湘
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  • 生命科学-已发表论文 [5901]
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Abstract
Aeromonas caviae can secrete several chintinases with different molecular weights. One chitinase gene chi1 has been cloned and sequenced. It encodes a protein of 865 amino acids with a signal peptide at the N-terminus, a polycystic kidney disease(PKD)-like domain, a triosephosphate isomerase(TIM) catalytic region, a receptor for egg jelly(REJ)-like domain and two tandem chitin binding domains (ChBDs). The entire chitinase degrades colloid chitin both endolytically and exolytically into N-acetylglucosamine, chitobiose and chitotriose. When removing the 302 amino acids at C-teminus its activity remains but the degraded products are chitobiose, chitotriose and chitotetraose. The study shows that for the full-length chitinase, its substrate with the shortest length is chitotriose while in its truncated form, it is chitotetraose.
Citation
PROGRESS IN NATURAL SCIENCE,vol12,issue8,pp587
URI
https://dspace.xmu.edu.cn/handle/2288/11056

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