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Difference between revisions of "Glycoside Hydrolase Family 114"
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== Substrate specificities == | == Substrate specificities == | ||
| − | Only a single enzyme of [[glycoside hydrolase]] family 114 has been characterized; an endo α-1,4-polygalactosaminidase from ''Pseudomonas'' sp. 881 <cite>Tamura1995</cite>. This enzyme hydrolyzes α-1,4-polygalactosamine to oligosaccharides in an endo-acting manner | + | Only a single enzyme of [[glycoside hydrolase]] family 114 has been characterized; an endo α-1,4-polygalactosaminidase from ''Pseudomonas'' sp. 881 <cite>Tamura1995</cite>. This enzyme hydrolyzes α-1,4-polygalactosamine to oligosaccharides in an [[endo]]-acting manner. α-1,4-Polygalactosamine, also known as galactosaminoglycan, is a polymer consisting of α-1,4-linked galactosamine residues, which is only partially ''N''-acetylated, and may also contain ''N''-formyl residues, and is produced by a range of fungi including ''Aspergillus parasiticus'', ''Paecilomyces'' sp. I-1, and ''Neurospora crassa''. An endogalactosaminidase has been purified from ''Streptomyces griseus''; the sequence of this protein is unknown <cite>Riessig1975</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | The endo α-1,4-polygalactosaminidase from ''Pseudomonas'' sp. 881 possesses activity on deacetylated α-1,4-polygalactosamine, but no activity on fully ''N''-acetylated α-1,4-polygalactosamine. | + | The endo α-1,4-polygalactosaminidase from ''Pseudomonas'' sp. 881 possesses activity on deacetylated α-1,4-polygalactosamine, but no activity on fully ''N''-acetylated α-1,4-polygalactosamine. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products <cite>Tamura1992</cite>. The enzyme is inhibited by |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 01:37, 3 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. α-1,4-Polygalactosamine, also known as galactosaminoglycan, is a polymer consisting of α-1,4-linked galactosamine residues, which is only partially N-acetylated, and may also contain N-formyl residues, and is produced by a range of fungi including Aspergillus parasiticus, Paecilomyces sp. I-1, and Neurospora crassa. An endogalactosaminidase has been purified from Streptomyces griseus; the sequence of this protein is unknown [2].
Kinetics and Mechanism
The endo α-1,4-polygalactosaminidase from Pseudomonas sp. 881 possesses activity on deacetylated α-1,4-polygalactosamine, but no activity on fully N-acetylated α-1,4-polygalactosamine. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products [3]. The enzyme is inhibited by
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 a retaining mechanism may be inferred from report of transglycosylation activity [3].
- First catalytic nucleophile identification
- Not known.
- First general acid/base residue identification
- Not known.
- First 3-D structure
- None reported.
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].
- Reissig JL, Lai WH, and Glasgow JE. (1975). An endogalactosaminidase from Streptomyces griseus. Can J Biochem. 1975;53(12):1237-49. DOI:10.1139/o75-169 |
- 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 |