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Difference between revisions of "Glycoside Hydrolase Family 114"
Harry Brumer (talk | contribs) (Assigned page to Spencer Williams) |
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| − | * [[Author]]: | + | * [[Author]]: ^^^Spencer Williams^^^ |
* [[Responsible Curator]]: ^^^Spencer Williams^^^ | * [[Responsible Curator]]: ^^^Spencer Williams^^^ | ||
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|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | | | + | |none |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | + | probably retaining | |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |not known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | + | Only a single enzyme of [[glycoside hydrolase]] family 114 has been characterized, with a single example of an endo α-1,4-polygalactosaminidase for an enzyme cloned from ''Pseudomonas'' sp. 881 <cite>Tamura1995</cite>. This enzyme hydrolyzes α-1,4-polygalactosamine to oligosaccharides in an endo-acting manner. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products <cite>Tamura1992</cite>. | |
| − | |||
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| Line 39: | Line 35: | ||
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | None known. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | No 3-D structure has been reported for any member of this family. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not known, but retaining may be inferred from report of transglycosylation activity <cite>Tamura1992</cite>. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: not known. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: not known. |
| − | ;First 3-D structure: | + | ;First 3-D structure: none. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Tamura1995 Tamura, J.-I., Hasegawa, K., Kadowaki, K., Igarashi, Y., Kodama, T. Molecular Cloning and Sequence Analysis of the Gene Encoding an Endo a-l,4 Polygalactosaminidase of Pseudomonas sp. 881. ''J. Fermentation Bioengineer.'', 1995, 80, 305. [http://dx.doi.org/10.1016/0922-338X(95)94196-X]. |
| − | + | ||
| + | #Tamura1992 pmid=27320986 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH114]] | [[Category:Glycoside Hydrolase Families|GH114]] | ||
Revision as of 14:09, 2 September 2016
- Author: ^^^Spencer Williams^^^
- Responsible Curator: ^^^Spencer Williams^^^
| Glycoside Hydrolase Family GH114 | |
| Clan | none |
| Mechanism
probably retaining | |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH114.html | |
Substrate specificities
Only a single enzyme of glycoside hydrolase family 114 has been characterized, with a single example of an endo α-1,4-polygalactosaminidase for an enzyme cloned from Pseudomonas sp. 881 [1]. This enzyme hydrolyzes α-1,4-polygalactosamine to oligosaccharides in an endo-acting manner. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products [2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
None known.
Three-dimensional structures
No 3-D structure has been reported for any member of this family.
Family Firsts
- First stereochemistry determination
- Not known, but retaining may be inferred from report of transglycosylation activity [2].
- First catalytic nucleophile identification
- not known.
- First general acid/base residue identification
- not known.
- First 3-D structure
- none.
References
-
Tamura, J.-I., Hasegawa, K., Kadowaki, K., Igarashi, Y., Kodama, T. Molecular Cloning and Sequence Analysis of the Gene Encoding an Endo a-l,4 Polygalactosaminidase of Pseudomonas sp. 881. J. Fermentation Bioengineer., 1995, 80, 305. [1].
- Tamura J, Abe T, Hasegawa K, and Kadowaki K. (1992). The Mode of Action of Endo α-1,4 Polygalactosaminidase from Pseudomonas sp. 881 on Galactosaminooligosaccharides. Biosci Biotechnol Biochem. 1992;56(3):380-3. DOI:10.1271/bbb.56.380 |