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Difference between revisions of "Glycoside Hydrolase Family 101"
| Line 25: | Line 25: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | The CAZY GH101 family currently contains proteins from 12 species of bacteria, most of which are commensal human bacteria, though some may also be human pathogens. The substrates are glycoproteins which contain the dissacharride Gal-beta-1,3-GalNAc-alpha-R ''O''-linked glycans on proteins. This glycosylation is a feature of mucin containing proteins. | + | The CAZY GH101 family currently contains proteins from 12 species of bacteria, most of which are commensal human bacteria, though some may also be human pathogens. The substrates are glycoproteins which contain the dissacharride Gal-beta-1,3-GalNAc-alpha-R ''O''-linked glycans on proteins. This glycosylation is a feature of mucin containing proteins. This enzyme activity was first observed in Clostridium <cite>1</cite> and then in Streptococcus pnuemoniae <cite>2</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | Retaining mechanism determined by H<sup>1</sup>-NMR with the BlGH101 enzyme <cite> | + | Retaining mechanism determined by H<sup>1</sup>-NMR with the BlGH101 enzyme <cite>3</cite>. |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | Using the enzyme from Streptococcus pnuemoniae the nucleophile was determined as residue D764. Willis et al in preparation <cite> | + | Using the enzyme from Streptococcus pnuemoniae the nucleophile was determined as residue D764. Willis et al in preparation <cite>4</cite> |
The acid/base catalyst in SpGH101 was determined to be E796. | The acid/base catalyst in SpGH101 was determined to be E796. | ||
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | <cite>5</cite>. <cite>6</cite> | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First sterochemistry determination: Cite some reference here, with a ''short'' explanation | + | ;First sterochemistry determination: Cite some reference here, with a ''short'' explanation. |
| − | This was determined with the BlGH101 enzyme using the H<sup>1</sup>-NMR technique. | + | This was determined with the BlGH101 enzyme using the H<sup>1</sup>-NMR technique <cite>3</cite>. |
;First catalytic nucleophile identification: | ;First catalytic nucleophile identification: | ||
| − | This was proposed based on the structure of the SpGH101 and BlGH101 structures, and then experimentally shown in SpGH101 by Willis and co-workers <cite> | + | This was proposed based on the structure of the SpGH101 and BlGH101 structures, and then experimentally shown in SpGH101 by Willis and co-workers <cite>4</cite>. |
;First general acid/base residue identification: | ;First general acid/base residue identification: | ||
| − | experimentally shown in SpGH101 by Willis and co-workers <cite> | + | experimentally shown in SpGH101 by Willis and co-workers <cite>4</cite> |
;First 3-D structure: | ;First 3-D structure: | ||
| − | Determined for SpGH101 by Caines and co-workers <cite> | + | Determined for SpGH101 by Caines and co-workers <cite>5</cite> |
== References == | == References == | ||
<biblio> | <biblio> | ||
Revision as of 10:17, 10 July 2009
| Glycoside Hydrolase Family GH101 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH101.html | |
Substrate specificities
The CAZY GH101 family currently contains proteins from 12 species of bacteria, most of which are commensal human bacteria, though some may also be human pathogens. The substrates are glycoproteins which contain the dissacharride Gal-beta-1,3-GalNAc-alpha-R O-linked glycans on proteins. This glycosylation is a feature of mucin containing proteins. This enzyme activity was first observed in Clostridium [1] and then in Streptococcus pnuemoniae [2].
Kinetics and Mechanism
Retaining mechanism determined by H1-NMR with the BlGH101 enzyme [3].
Catalytic Residues
Using the enzyme from Streptococcus pnuemoniae the nucleophile was determined as residue D764. Willis et al in preparation [4] The acid/base catalyst in SpGH101 was determined to be E796.
Three-dimensional structures
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short explanation.
This was determined with the BlGH101 enzyme using the H1-NMR technique [3].
- First catalytic nucleophile identification
This was proposed based on the structure of the SpGH101 and BlGH101 structures, and then experimentally shown in SpGH101 by Willis and co-workers [4].
- First general acid/base residue identification
experimentally shown in SpGH101 by Willis and co-workers [4]
- First 3-D structure
Determined for SpGH101 by Caines and co-workers [5]
References
- Bhavanandan VP, Umemoto J, and Davidson EA. (1976). Characterization of an endo-alpha-N-acetyl galactosaminidase from Diplococcus pneumoniae. Biochem Biophys Res Commun. 1976;70(3):738-45. DOI:10.1016/0006-291x(76)90654-9 |
- Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, and Yamamoto K. (2005). Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. J Biol Chem. 2005;280(45):37415-22. DOI:10.1074/jbc.M506874200 |
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pmid=
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pmid=
- Caines ME, Zhu H, Vuckovic M, Willis LM, Withers SG, Wakarchuk WW, and Strynadka NC. (2008). The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design. J Biol Chem. 2008;283(46):31279-83. DOI:10.1074/jbc.C800150200 |
- Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, and Fushinobu S. (2009). Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. J Biochem. 2009;146(3):389-98. DOI:10.1093/jb/mvp086 |