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Difference between revisions of "Glycoside Hydrolase Family 114"
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|'''Active site residues''' | |'''Active site residues''' |
Revision as of 14:10, 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; an endo α-1,4-polygalactosaminidase 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 |