RRC ID |
4806
|
Author |
Dedeurwaerder S, Menu-Bouaouiche L, Mareck A, Lerouge P, Guerineau F.
|
Title |
Activity of an atypical Arabidopsis thaliana pectin methylesterase.
|
Journal |
Planta
|
Abstract |
An Arabidopsis thaliana pectin methylesterase that was not predicted to contain any signaling sequence was produced in E. coli and purified using a His tag added at its N-terminus. The enzyme demethylesterified Citrus pectin with a Km of 0.86 mg/ml. The enzyme did not require salt for activity and was found to be relatively temperature-sensitive. The precipitation of enzyme-treated pectin by CaCl2 suggested that the enzyme had a blockwise mode of pectin demethylesterification. A purified kiwi (Actinidia chinensis) pectin methylesterase inhibitor had no effect on the activity of the enzyme whereas it strongly inhibited a flax pectin methylesterase. A model of the protein structure revealed that an extra amino acid sequence in this particular Arabidopsis pectin methylesterase could form a ss-strand outside the core structure, which might be preventing the inhibitor from binding the protein.
|
Volume |
229(2)
|
Pages |
311-21
|
Published |
2009-1-1
|
DOI |
10.1007/s00425-008-0831-0
|
PMID |
18936961
|
MeSH |
Actinidia / enzymology
Amino Acid Sequence
Arabidopsis / drug effects
Arabidopsis / enzymology*
Arabidopsis Proteins / antagonists & inhibitors
Arabidopsis Proteins / chemistry
Arabidopsis Proteins / isolation & purification
Arabidopsis Proteins / metabolism*
Carboxylic Ester Hydrolases / antagonists & inhibitors
Carboxylic Ester Hydrolases / chemistry
Carboxylic Ester Hydrolases / isolation & purification
Carboxylic Ester Hydrolases / metabolism*
Catalytic Domain
Electrophoresis, Polyacrylamide Gel
Enzyme Inhibitors / pharmacology
Models, Molecular
Molecular Sequence Data
Protein Structure, Secondary
Sequence Alignment
Sequence Analysis, Protein
|
IF |
3.39
|
Times Cited |
17
|
WOS Category
|
PLANT SCIENCES
|
Resource |
Arabidopsis / Cultured plant cells, genes |
pda06543 |