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Difference between revisions of "Glycoside Hydrolase Family 63"
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== Substrate specificities == | == Substrate specificities == | ||
− | Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosacharide precursor, Glc<sub>3</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>. The enzymatic properties of Cwh41p, a processing α glucosidase I from ''Saccharomyces cerevisiae'', has been most intensively studied. | + | Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the ''N''-linked oligosacharide precursor, Glc<sub>3</sub>Man<sub>9</sub>GlcNAc<sub>2</sub>. The enzymatic properties of Cwh41p, a processing α glucosidase I from ''Saccharomyces cerevisiae'', has been most intensively studied. |
Revision as of 02:13, 20 April 2011
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- Author: ^^^Takashi Tonozuka^^^
- Responsible Curator: ^^^Takashi Tonozuka^^^
Glycoside Hydrolase Family GH63 | |
Clan | GH-G |
Mechanism | inverting |
Active site residues | not known |
CAZy DB link | |
https://www.cazy.org/GH63.html |
Substrate specificities
Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing α-glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal α-1,2-glucosidic linkage in the N-linked oligosacharide precursor, Glc3Man9GlcNAc2. The enzymatic properties of Cwh41p, a processing α glucosidase I from Saccharomyces cerevisiae, has been most intensively studied.
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [1].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
References
Error fetching PMID 9312086:
- Error fetching PMID 17323919:
- Error fetching PMID 9312086:
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006