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
Search PMC articles PubMed articles NCBI proteins

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

D-glucopyranosyl abscisate + H²O $\rightleftharpoons$ D-glucose + abscisate

The enzyme hydrolzes the biologically inactive beta-D-glucopyranosyl ester of abscisic acid to produce active abscisate.

References

1. Lee, K.H., Piao, H.L., Kim, H.Y., Choi, S.M., Jiang, F., Hartung, W., Hwang, I., Kwak, J.M., Lee, I.J. and 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.
2. Kato-Noguchi, H. and 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.
3. Dietz, K.J., Sauter, A., Wichert, K., Messdaghi, D. and 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)