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Difference between revisions of "Glycoside Hydrolase Family 128"
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− | Family GH128 contains β-1,3-glucanases that cleave β-1,3 linkages in various β-glucans such as lentinan from ''Lentinula edodes'', laminarin from ''Laminaria digitata'', pachyman from ''Poria cocos'' and curdlan from ''Alcaligenes faecalis''. The first GH128 enzyme, GLU1, was cloned from ''L. edodes'' fruiting bodies (shiitake mushroom). GLU1 did not degrade β-1,3-linkages within β-1,3-1,4-glucans such as barley glucan, indicating the enzyme is categorized into (EC [{{EClink}}3.2.1.39 3.2.1.39]) | + | Family GH128 contains β-1,3-glucanases that cleave β-1,3 linkages in various β-glucans such as lentinan from ''Lentinula edodes'', laminarin from ''Laminaria digitata'', pachyman from ''Poria cocos'' and curdlan from ''Alcaligenes faecalis''. The first GH128 enzyme, GLU1, was cloned from ''L. edodes'' fruiting bodies (shiitake mushroom). GLU1 did not degrade β-1,3-linkages within β-1,3-1,4-glucans such as barley glucan, indicating the enzyme is categorized into (EC [{{EClink}}3.2.1.39 3.2.1.39]) <cite>Sakamoto2011</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == |
Revision as of 20:05, 21 July 2015
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Yuichi Sakamoto^^^
- Responsible Curator: ^^^Yuichi Sakamoto^^^
Glycoside Hydrolase Family GH128 | |
Clan | GH-x |
Mechanism | retaining/inverting |
Active site residues | known/not known |
CAZy DB link | |
http://www.cazy.org/GH128.html |
Substrate specificities
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Family GH128 contains β-1,3-glucanases that cleave β-1,3 linkages in various β-glucans such as lentinan from Lentinula edodes, laminarin from Laminaria digitata, pachyman from Poria cocos and curdlan from Alcaligenes faecalis. The first GH128 enzyme, GLU1, was cloned from L. edodes fruiting bodies (shiitake mushroom). GLU1 did not degrade β-1,3-linkages within β-1,3-1,4-glucans such as barley glucan, indicating the enzyme is categorized into (EC 3.2.1.39) [1].
Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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