The role of active site aromatic residues in substrate degradation by the human chitotriosidase
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- 作者：Kristine Bistrup Eidea ; 1 ; Linn Wilhelmsen Stockingera ; 1 ; Anna Sofia Lewinb ; Anne Tø ; ndervikb ; Vincent G.H. Eijsinka ; Morten Sø ; rliea ; morten.sorlie@nmbu.no" class="auth_mail" title="E-mail the corresponding author
- 关键词：HCHT ; human chitotriosidase ; HCHT50 ; the 50 ; kDa variant of HCHT ; HCHT39 ; the 39 ; kDa variant of HCHT ; AMCase ; acidic mammalian chitinase ; GH ; glycoside hydrolase ; GlcNAc (A) ; 2-acetamido-2-deoxy-β-D-glucopyranose ; GlcN (D) ; 2-amino-2-deoxy-β-D-glucopyranose ; CBM ; carbohydrate-binding module ; 4-MU ; 4-methylumbelliferyl ; DP ; degree of polymerization ; MBTH ; 3-methyl-2- benzothiazolinone hydrazine ; α ; the degree of scission ; Fa ; fraction of acetylated sugar moieties
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：1864
- 期：2
- 页码：242-247
- 全文大小：651 K
文摘
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Human chitotriosidase (HCHT) activity depend on surface exposed aromatic residues
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Processive ability, catalytic efficiency on insoluble substrates may not be connected
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HCHT50 shows atypical properties relative to bacterial enzymes