Glycoside hydrolase family 28

Glycosyl hydrolases family 28
rhamnogalacturonase a from aspergillus aculeatus
Identifiers
Symbol	Glyco_hydro_28
Pfam	PF00295
Pfam clan	CL0268
InterPro	IPR000743
PROSITE	PDOC00415
SCOP2	1rmg / SCOPe / SUPFAM
CAZy	GH28
Membranome	73
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, glycoside hydrolase family 28 is a family of glycoside hydrolases EC 3.2.1., which 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 28 CAZY GH_28 comprises enzymes with several known activities; polygalacturonase (EC 3.2.1.15); exo-polygalacturonase (EC 3.2.1.67); exo-polygalacturonase (EC 3.2.1.82); rhamnogalacturonase (EC not defined).

Polygalacturonase (PG) (pectinase) ^{[8] [9]} catalyzes the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans. In fruit, polygalacturonase plays an important role in cell wall metabolism during ripening. In plant bacterial pathogens such as Erwinia carotovora or Ralstonia solanacearum (Pseudomonas solanacearum) and fungal pathogens such as Aspergillus niger , polygalacturonase is involved in maceration and soft-rotting of plant tissue. Exo-poly-alpha-D-galacturonosidase (EC 3.2.1.82) (exoPG) ^[10] hydrolyzes peptic acid from the non-reducing end, releasing digalacturonate. PG and exoPG share a few regions of sequence similarity, and belong to family 28 of the glycosyl hydrolases.

References

1. 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.
2. 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.
3. 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.
4. "Home". CAZy.org. Retrieved 2018-03-06.
5. 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.
6. "Glycoside Hydrolase Family 28". CAZypedia.org. Retrieved 2018-03-06.
7. 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.
8. Ruttkowski E, Labitzke R, Khanh NQ, Löffler F, Gottschalk M, Jany KD (September 1990). "Cloning and DNA sequence analysis of a polygalacturonase cDNA from Aspergillus niger RH5344". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1087 (1): 104–6. doi:10.1016/0167-4781(90)90130-t. PMID   2400785.
9. Huang JH, Schell MA (July 1990). "DNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum". Journal of Bacteriology. 172 (7): 3879–87. doi:10.1128/jb.172.7.3879-3887.1990. PMC   213369 . PMID   2193922.
10. He SY, Collmer A (September 1990). "Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16". Journal of Bacteriology. 172 (9): 4988–95. doi:10.1128/jb.172.9.4988-4995.1990. PMC   213154 . PMID   2168372.

This article incorporates text from the public domain Pfam and InterPro: IPR000743