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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 &alpha; glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal &alpha;-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 &alpha; glucosidase I from ''Saccharomyces cerevisiae'', has been most intensively studied.
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Glycoside hydrolases of this family are exo-acting inverting enzymes. The most commonly characterized activity of the eukaryotic enzymes is processing &alpha;-glucosidase I (EC 3.2.1.106), which specifically hydrolyzes the terminal &alpha;-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 &alpha; glucosidase I from ''Saccharomyces cerevisiae'', has been most intensively studied.
  
  

Revision as of 02:13, 20 April 2011

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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 17323919:
Error fetching PMID 9312086:
  1. Error fetching PMID 17323919: [Comfort2007]
  2. Error fetching PMID 9312086: [He1999]
  3. [StickWilliams]
  4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [Sinnott1990]

All Medline abstracts: PubMed