NDLI: Characterization of trimeric acetylcholinesterase from a legume plant, Macroptilium atropurpureum Urb.

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Planta : Volume 227, Issue 3, February 2008

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Planta : Volume 227, Issue 1, December 2007

Characterization of trimeric acetylcholinesterase from a legume plant, Macroptilium atropurpureum Urb.

Content Provider	Springer Nature Link
Author	Yamamoto, Kosuke Oguri, Suguru Momoki, Yoshie S.
Copyright Year	2007
Abstract	We recently identified plant acetylcholinesterases (E.C.3.1.1.7; AChEs) homologous to the AChE purified from a monocotyledon, maize, that are distinct from the animal AChE family. In this study, we purified, cloned and characterized an AChE from a dicotyledon, siratro. The full-length cDNA of siratro AChE is 1,441 nucleotides, encoding a 382-residue protein that includes a signal peptide. This AChE is a disulfide-linked 125-kDa homotrimer consisting of 41–42 kDa subunits, in contrast to the maize AChE, which exists as a mixture of disulfide and non-covalently linked 88-kDa homodimers. The plant AChEs apparently consist of various quaternary structures, depending on the plant species, similar to the animal AChEs. We compared the enzymatic properties of the dimeric maize and trimeric siratro AChEs. Similar to electric eel AChE, both plant AChEs hydrolyzed acetylthiocholine (or acetylcholine) and propionylthiocholine (or propionylcholine), but not butyrylthiocholine (or butyrylcholine), and their specificity constant was highest against acetylcholine. There was no significant difference between the enzymatic properties of trimeric and dimeric AChEs, although two plant AChEs had low substrate turnover numbers compared with electric eel AChE. The two plant AChE activities were not inhibited by excess substrate concentrations. Thus, similar to some plant AChEs, siratro and maize AChEs showed enzymatic properties of both animal AChE and animal BChE. On the other hand, both siratro and maize AChEs exhibited low sensitivity to the AChE-specific inhibitor neostigmine bromide, dissimilar to other plant AChEs. These differences in enzymatic properties of plant AChEs may reflect the phylogenetic evolution of AChEs.
Starting Page	809
Ending Page	822
Page Count	14
File Format	PDF
ISSN	00320935
Journal	Planta
Volume Number	227
Issue Number	4
e-ISSN	14322048
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-11-28
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Acetylcholine-mediated system Acetylcholinesterase Legume plant Macroptilium atropurpureum Urb. Trimeric siratro AChE Forestry Ecology Agriculture Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Genetics Plant Science

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Characterization of trimeric acetylcholinesterase from a legume plant, Macroptilium atropurpureum Urb.

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