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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. 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 | + | 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 fungi including ''Aspergillus parasiticus'' and ''Paecilomyces'' sp. I-1. 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. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products <cite>Tamura1992</cite>. The enzyme is inhibited by | + | 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 <cite>#Tamura1988</cite>. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products <cite>Tamura1992</cite>. Based on the dependence of rate on the chain length of the substrate, it was proposed that the enzyme has 8 subsites <cite>Tamura1992</cite> The enzyme is inhibited by metal ions including Hg<sup>2+</sup>, Fe<sup>2+</sup> and Sn<sup>2+</sup> <cite>#Tamura1988</cite>. |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 49: | Line 49: | ||
<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]. | #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 | #Tamura1992 pmid=27320986 | ||
#Riessig1975 pmid=3271 | #Riessig1975 pmid=3271 | ||
| + | #Tamura1988 Tamura, J.-I., Takagi, H., Kadowaki, K. Purification and Some Properties of the Endo α-1,4 Polygalactosaminidase from Pseudomonas sp., ''Agric. Biol. Chem.'' 1988, 52 , 2475-2484. [http://dx.doi.org/10.1080/00021369.1988.10869068]. | ||
| + | |||
| + | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH114]] | [[Category:Glycoside Hydrolase Families|GH114]] | ||
Revision as of 02:49, 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 | |
| http://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 fungi including Aspergillus parasiticus and Paecilomyces sp. I-1. 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 [3]. Tetraose and longer galactosamine oligosaccharides were hydrolyzed to galactosaminobiose and galactosaminotriose as the final products [4]. Based on the dependence of rate on the chain length of the substrate, it was proposed that the enzyme has 8 subsites [4] The enzyme is inhibited by metal ions including Hg2+, Fe2+ and Sn2+ [3].
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 [4].
- 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.-I., Takagi, H., Kadowaki, K. Purification and Some Properties of the Endo α-1,4 Polygalactosaminidase from Pseudomonas sp., Agric. Biol. Chem. 1988, 52 , 2475-2484. [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 |