Glycoside hydrolase family 27

Melibiase

crystal structure of rice alpha-galactosidase

Identifiers
Symbol| Melibiase
Pfam| PF02065
Pfam clan| CL0058
InterPro| IPR000111
SCOP2| 1ktc / SCOPe / SUPFAM
CAZy| GH27
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

In molecular biology, glycoside hydrolase family 27 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 27 together with family 31 and the family 36 alpha-galactosidases form the glycosyl hydrolase clan GH-D, a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a common catalytic mechanism and structural topology.

Alpha-galactosidase (EC 3.2.1.22) (melibiase)[8] catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). Alpha-galactosidase is present in a variety of organisms. There is a considerable degree of similarity in the sequence of alpha-galactosidase from various eukaryotic species. Escherichia coli alpha-galactosidase (gene melA), which requires NAD and magnesium as cofactors, is not structurally related to the eukaryotic enzymes; by contrast, an Escherichia coli plasmid encoded alpha-galactosidase (gene rafA P16551)[9] contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases. Alpha-N-acetylgalactosaminidase (EC 3.2.1.49)[10] catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D- galactosaminides. In man, the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases. The sequence of this enzyme is highly related to that of the eukaryotic alpha-galactosidases.

## External links[edit]

* GH27 in CAZypedia

## References[edit]

1. ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
2. ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
3. ^ "Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999". Archived from the original on 2011-05-25. Retrieved 2011-10-04.
4. ^ "Home". CAZy.org. Retrieved 2018-03-06.
5. ^ Lombard, Vincent; Golaconda Ramulu, Hemalatha; Drula, Elodie; Coutinho, Pedro M.; Henrissat, Bernard (2014-01-01). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (D1): D490–D495. doi:10.1093/nar/gkt1178. ISSN 0305-1048. PMC 3965031. PMID 24270786.
6. ^ "Glycoside Hydrolase Family 27". CAZypedia.org. Retrieved 2018-03-06.
7. ^ CAZypedia Consortium (2018-12-01). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. ISSN 1460-2423. PMID 29040563.
8. ^ Dey PM, Pridham JB (1972). "Biochemistry of α‐Galactosidases". Advances in Enzymology and Related Areas of Molecular Biology. pp. 91–120. doi:10.1002/9780470122815.ch3. ISBN 9780470122815. PMID 4561015. `{{cite book}}`: `|journal=` ignored (help)
9. ^ Aslanidis C, Schmid K, Schmitt R (1989). "Nucleotide sequences and operon structure of plasmid-borne genes mediating uptake and utilization of raffinose in Escherichia coli". J. Bacteriol. 171 (12): 6753–6763. doi:10.1128/jb.171.12.6753-6763.1989. PMC 210573. PMID 2556373.
10. ^ Wang AM, Bishop DF, Desnick RJ (1990). "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene". J. Biol. Chem. 265 (35): 21859–21866. doi:10.1016/S0021-9258(18)45818-8. PMID 2174888.

This article incorporates text from the public domain Pfam and InterPro: IPR000111

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Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases|

| Disaccharidase|

* Sucrase/Sucrase-isomaltase/Invertase
* Maltase
* Trehalase
* Lactase

|

Glucosidases|

* Cellulase
* Alpha-glucosidase
* Acid
* Neutral AB
* Neutral C
* Beta-glucosidase
* cytosolic
* Debranching enzyme

Other|

* Amylase
* Alpha-amylase
* Chitinase
* Lysozyme
* Neuraminidase
* NEU1
* NEU2
* NEU3
* NEU4
* Bacterial neuraminidase
* Viral neuraminidase
* Galactosidases
* Alpha
* Beta
* alpha-Mannosidase
* Glucuronidase
* Klotho
* Hyaluronidase
* Pullulanase
* Glucosylceramidase
* lysosomal
* non-lysosomal
* Galactosylceramidase
* Alpha-N-acetylgalactosaminidase
* NAGA
* Alpha-N-acetylglucosaminidase
* Fucosidase
* Hexosaminidase
* HEXA
* HEXB
* Iduronidase
* Maltase-glucoamylase
* Heparanase
* HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds|

* DNA glycosylases: Oxoguanine glycosylase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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* Biology

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