Beta-D-glucopyranosyl abscisate beta-glucosidase
| Beta-D-glucopyranosyl abscisate beta-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.175 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Beta-D-glucopyranosyl abscisate beta-glucosidase (EC 3.2.1.175, AtBG1, ABA-beta-D-glucosidase, ABA-specific beta-glucosidase, ABA-GE hydrolase, beta-D-glucopyranosyl abscisate hydrolase) is an enzyme with systematic name beta-D-glucopyranosyl abscisate glucohydrolase.[1][2][3] This enzyme catalyses the following chemical reaction
The enzyme hydrolzes the biologically inactive beta-D-glucopyranosyl ester of abscisic acid to produce active abscisate.
References
- ↑ Lee, K.H.; Piao, H.L.; Kim, H.Y.; Choi, S.M.; Jiang, F.; Hartung, W.; Hwang, I.; Kwak, J.M.; Lee, I.J.; Hwang, I. (2006). "Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid". Cell. 126: 1109–1120. doi:10.1016/j.cell.2006.07.034. PMID 16990135.
- ↑ Kato-Noguchi, H.; Tanaka, Y. (2008). "Effect of ABA-β-D-glucopyranosyl ester and activity of ABA-β-D-glucosidase in Arabidopsis thaliana". J. Plant Physiol. 165: 788–790. doi:10.1016/j.jplph.2007.04.005. PMID 17923167.
- ↑ Dietz, K.J.; Sauter, A.; Wichert, K.; Messdaghi, D.; Hartung, W. (2000). "Extracellular β-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves". J. Exp. Bot. 51 (346): 937–944. doi:10.1093/jexbot/51.346.937. PMID 10948220.
External links
- Beta-D-glucopyranosyl abscisate beta-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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