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Difference between revisions of "Glycoside Hydrolase Family 29"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
GH29 α-fucosidases  are [[retaining]] enzymes following a classical Koshland double-displacement mechanism, as first proposed in 1987 for human liver α-fucosidase via burst kinetics experiments and  using methanol as an alternative glycone acceptor to produce methyl-α-L-fucoside (White et al, Biochim. Biophys. Acta 912, 132–138, PMID: 3828350). This has been further confirmed by 1H NMR monitoring of the reaction catalyzed by α-L-fucosidase from Thermus sp. (Eneyskaya et al. Glycoconj. J. 18, 827–834 PMID: 12441672) and α-L-fucosidase from the marine mollusc Pecten maximus (Berteau et al., Glycobiology 12, 273–282 PMID: 12042250), as well as by COSY and 1H-13C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation action of Sulfolobus solfataricus α-L-fucosidase (PMID: 12569098). GH95 α-fucosidases, in contrast, operate with inversion of the anomeric configuration.
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GH29 α-fucosidases  are [[retaining]] enzymes following a classical Koshland double-displacement mechanism, as first proposed in 1987 for human liver α-fucosidase via burst kinetics experiments and  using methanol as an alternative glycone acceptor to produce methyl-α-L-fucoside <cite>2</cite>.(White et al, Biochim. Biophys. Acta 912, 132–138, PMID: 3828350). This has been further confirmed by 1H NMR monitoring of the reaction catalyzed by α-L-fucosidase from Thermus sp. (Eneyskaya et al. Glycoconj. J. 18, 827–834 PMID: 12441672) and α-L-fucosidase from the marine mollusc Pecten maximus (Berteau et al., Glycobiology 12, 273–282 PMID: 12042250), as well as by COSY and 1H-13C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation action of Sulfolobus solfataricus α-L-fucosidase (PMID: 12569098). GH95 α-fucosidases, in contrast, operate with inversion of the anomeric configuration.
  
  
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<biblio>
 
<biblio>
 
#1 pmid=2894306
 
#1 pmid=2894306
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#2 pmid=3828350
  
  

Revision as of 05:27, 17 December 2009

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH 29
Clan none
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH29.html


Substrate specificities

The glycoside hydrolases of this family are exo-acting α-fucosidases from archaeal, bacterial and eukaryotic origin. No other activities have been observed for GH29 family members. So fare the only other CAZY family containing α-fucosidases is family GH95. The human enzyme FucA1 is of medical interest because its deficiency leads to fucosidosis, an autosomal recessive lysosomal storage disease [1].


Kinetics and Mechanism

GH29 α-fucosidases are retaining enzymes following a classical Koshland double-displacement mechanism, as first proposed in 1987 for human liver α-fucosidase via burst kinetics experiments and using methanol as an alternative glycone acceptor to produce methyl-α-L-fucoside [2].(White et al, Biochim. Biophys. Acta 912, 132–138, PMID: 3828350). This has been further confirmed by 1H NMR monitoring of the reaction catalyzed by α-L-fucosidase from Thermus sp. (Eneyskaya et al. Glycoconj. J. 18, 827–834 PMID: 12441672) and α-L-fucosidase from the marine mollusc Pecten maximus (Berteau et al., Glycobiology 12, 273–282 PMID: 12042250), as well as by COSY and 1H-13C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the transglycosylation action of Sulfolobus solfataricus α-L-fucosidase (PMID: 12569098). GH95 α-fucosidases, in contrast, operate with inversion of the anomeric configuration.


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.


Family Firsts

First sterochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [3].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [4].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [6].

References

  1. O'Brien JS, Willems PJ, Fukushima H, de Wet JR, Darby JK, Di Cioccio R, Fowler ML, and Shows TB. (1987). Molecular biology of the alpha-L-fucosidase gene and fucosidosis. Enzyme. 1987;38(1-4):45-53. DOI:10.1159/000469189 | PubMed ID:2894306 [1]
  2. White WJ Jr, Schray KJ, Legler G, and Alhadeff JA. (1987). Further studies on the catalytic mechanism of human liver alpha-L-fucosidase. Biochim Biophys Acta. 1987;912(1):132-8. DOI:10.1016/0167-4838(87)90256-1 | PubMed ID:3828350 [2]

All Medline abstracts: PubMed

[[Category:Glycoside Hydrolase Families|GHnnn]]