Beta-D-glucopyranosyl abscisate beta-glucosidase
(Redirected from ABA-GE hydrolase)
| Beta-D-glucopyranosyl abscisate beta-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 hydrolyzes the biologically inactive beta-D-glucopyranosyl ester of abscisic acid to produce active abscisate.
References
[edit]- ^ Lee KH, Piao HL, Kim HY, Choi SM, Jiang F, Hartung W, Hwang I, Kwak JM, Lee IJ, Hwang I (September 2006). "Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid". Cell. 126 (6): 1109–20. doi:10.1016/j.cell.2006.07.034. PMID 16990135.
- ^ Kato-Noguchi H, Tanaka Y (May 2008). "Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-glucosidase in Arabidopsis thaliana". Journal of Plant Physiology. 165 (7): 788–90. doi:10.1016/j.jplph.2007.04.005. PMID 17923167.
- ^ Dietz KJ, Sauter A, Wichert K, Messdaghi D, Hartung W (May 2000). "Extracellular beta-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves". Journal of Experimental Botany. 51 (346): 937–44. doi:10.1093/jexbot/51.346.937. PMID 10948220.
External links
[edit]- Beta-D-glucopyranosyl+abscisate+beta-glucosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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