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Glycoside Hydrolase Family 53
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- Author: ^^^Leila Lo Leggio^^^
- Responsible Curator: ^^^Leila Lo Leggio^^^
| Glycoside Hydrolase Family GH53 | |
| Clan | GH-A |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH53.html | |
Substrate specificities
The only known specificity for this family is beta-1,4-galactanase (EC 3.2.1.89) and the only reported function is the microbial degradation of galactans and arabinogalactans in the pectic component of plant cell walls. A number of patents on industrial applications of GH53 have been filed.
Kinetics and Mechanism
GH53 beta-1,4-galactanases follow a classical retaining mechanism (Ref.). Most characterized members have been reported to have an endo-mode of action (refs), although processivity has been suggested in one case (Ref).
Catalytic Residues
Two glutamates act as catalytic residues, as nucleophile and acid-base catalyst respectively, and were first identified by Braithwhite et al,.
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 [1].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [3].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [4].
References
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- Error fetching PMID 9312086:
- Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.