Glycoside hydrolase family 29: Difference between revisions
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Glycoside hydrolase family 29 includes [[alpha-L-fucosidase]]s,<ref name="pmid2482732">{{cite journal | vauthors = Fisher KJ, Aronson NN | title = Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase | journal = The Biochemical Journal | volume = 264 | issue = 3 | pages = 695–701 | date = December 1989 | pmid = 2482732 | pmc = 1133642 | doi = 10.1042/bj2640695}}</ref> They are [[lysosome|lysosomal]] enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate [[Moiety (chemistry)|moieties]] of [[glycoproteins]]. [[Alpha-L-fucosidase]] is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of [[glycoprotein]]s. |
Glycoside hydrolase family 29 includes [[alpha-L-fucosidase]]s,<ref name="pmid2482732">{{cite journal | vauthors = Fisher KJ, Aronson NN | title = Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase | journal = The Biochemical Journal | volume = 264 | issue = 3 | pages = 695–701 | date = December 1989 | pmid = 2482732 | pmc = 1133642 | doi = 10.1042/bj2640695}}</ref> They are [[lysosome|lysosomal]] enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate [[Moiety (chemistry)|moieties]] of [[glycoproteins]]. [[Alpha-L-fucosidase]] is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of [[glycoprotein]]s. |
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Fucosylated glycoconjugates are involved in numerous [[biology|biological]] events, making alpha-l-fucosidases, the [[enzymes]] responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with [[fucosidosis]], a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.<ref name="pmid14715651">{{cite journal | vauthors = Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y | title = Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis | journal = The Journal of Biological Chemistry | volume = 279 | issue = 13 | pages = 13119–28 | date = March 2004 | pmid = 14715651 | doi = 10.1074/jbc.M313783200 | doi-access = free }}</ref> The enzyme is a hexamer and displays a two-domain fold, composed of a [[catalytic]] (beta/alpha)(8)-like domain and a C-terminal [[beta-sandwich]] domain.<ref name="pmid14715651"/> |
Fucosylated glycoconjugates are involved in numerous [[biology|biological]] events, making alpha-l-fucosidases, the [[enzymes]] responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with [[fucosidosis]], a [[lysosomal storage disorder]] characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.<ref name="pmid14715651">{{cite journal | vauthors = Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y | title = Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis | journal = The Journal of Biological Chemistry | volume = 279 | issue = 13 | pages = 13119–28 | date = March 2004 | pmid = 14715651 | doi = 10.1074/jbc.M313783200 | doi-access = free }}</ref> The enzyme is a hexamer and displays a two-domain fold, composed of a [[catalytic]] (beta/alpha)(8)-like domain and a C-terminal [[beta-sandwich]] domain.<ref name="pmid14715651"/> |
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''[[Drosophila]] melanogaster'' [[spermatozoa]] contains an alpha-l-fucosidase that might be involved in [[fertilisation]] by interacting with alpha-l-fucose residues on the micropyle of the eggshell.<ref name="pmid18556148">{{cite journal | vauthors = Pasini ME, Intra J, Pavesi G | title = Expression study of an alpha-l-fucosidase gene in the Drosophilidae family | journal = Gene | volume = 420 | issue = 1 | pages = 23–33 | date = August 2008 | pmid = 18556148 | doi = 10.1016/j.gene.2008.04.021 }}</ref> In [[Homo sapiens|human]] sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by [[Cell membrane|membrane]] [[protein domain|domains]] and compartmentalisation. These help preserve protein integrity.<ref name="pmid18522672">{{cite journal | vauthors = Venditti JJ, Bean BS | title = Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment | journal = International Journal of Andrology | volume = 32 | issue = 5 | pages = 556–62 | date = October 2009 | pmid = 18522672 | doi = 10.1111/j.1365-2605.2008.00897.x | doi-access = free }}</ref> |
''[[Drosophila]] melanogaster'' [[spermatozoa]] contains an alpha-l-fucosidase that might be involved in [[fertilisation]] by interacting with alpha-l-fucose residues on the micropyle of the eggshell.<ref name="pmid18556148">{{cite journal | vauthors = Pasini ME, Intra J, Pavesi G | title = Expression study of an alpha-l-fucosidase gene in the Drosophilidae family | journal = Gene | volume = 420 | issue = 1 | pages = 23–33 | date = August 2008 | pmid = 18556148 | doi = 10.1016/j.gene.2008.04.021 }}</ref> In [[Homo sapiens|human]] sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by [[Cell membrane|membrane]] [[protein domain|domains]] and compartmentalisation. These help preserve protein integrity.<ref name="pmid18522672">{{cite journal | vauthors = Venditti JJ, Bean BS | title = Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment | journal = International Journal of Andrology | volume = 32 | issue = 5 | pages = 556–62 | date = October 2009 | pmid = 18522672 | doi = 10.1111/j.1365-2605.2008.00897.x | doi-access = free }}</ref> |
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Revision as of 19:42, 12 May 2024
| Alpha-L-fucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of thermotoga maritima alpha-fucosidase | |||||||||
| Identifiers | |||||||||
| Symbol | Alpha_L_fucos | ||||||||
| Pfam | PF01120 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR000933 | ||||||||
| PROSITE | PDOC00324 | ||||||||
| SCOP2 | 1hl9 / SCOPe / SUPFAM | ||||||||
| CAZy | GH29 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]
Glycoside hydrolase family 29 includes alpha-L-fucosidases,[8] They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.[9] The enzyme is a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain.[9]
Drosophila melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilisation by interacting with alpha-l-fucose residues on the micropyle of the eggshell.[10] In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. These help preserve protein integrity.[11]
References
- ^ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ^ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 (Pt 2): 695–6. doi:10.1042/bj3160695. PMC 1217404. PMID 8687420.
- ^ "Home". CAZy.org. Retrieved 2018-03-06.
- ^ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490-5. doi:10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
- ^ "Glycoside Hydrolase Family 29". CAZypedia.org. Retrieved 2018-03-06.
- ^ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563.
- ^ Fisher KJ, Aronson NN (December 1989). "Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase". The Biochemical Journal. 264 (3): 695–701. doi:10.1042/bj2640695. PMC 1133642. PMID 2482732.
- ^ a b Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y (March 2004). "Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis". The Journal of Biological Chemistry. 279 (13): 13119–28. doi:10.1074/jbc.M313783200. PMID 14715651.
- ^ Pasini ME, Intra J, Pavesi G (August 2008). "Expression study of an alpha-l-fucosidase gene in the Drosophilidae family". Gene. 420 (1): 23–33. doi:10.1016/j.gene.2008.04.021. PMID 18556148.
- ^ Venditti JJ, Bean BS (October 2009). "Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment". International Journal of Andrology. 32 (5): 556–62. doi:10.1111/j.1365-2605.2008.00897.x. PMID 18522672.
