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Partial purification and identification of GDP-mannose 3", 5"-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway

Beata Wolucka UGent, Geert Persiau UGent, Jan Van Doorsselaere UGent, Mark W Davey UGent, Hans Demol UGent, Joël Vandekerckhove, Marc Van Montagu UGent, Marc Zabeau and Wout Boerjan UGent (2001) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 98(26). p.14843-14848
abstract
The first step in the biosynthetic pathway of vitamin C in plants is the formation, at the level of sugar nucleotide, Of L-galactosyl residues, catalyzed by a largely unknown GDP-D-mannose 3 " ,5 " -epimerase. By using combined conventional biochemical and mass spectrometry methods, we obtained a highly purified preparation of GDP-D-mannose 3 " ,5 " -epimerase from an Arabidopsis thaliana cell suspension. The native enzyme is an 84-kDa dimer, composed of two apparently identical subunits. In-gel tryptic digestion of the enzyme subunit, followed by peptide sequencing and a BLAST search, led to the identification of the epimerase gene. The closest homolog of the plant epimerase is the BlmG gene product of Streptomyces sp., a putative NDP-D-mannose 5 " -epimerase. The plant GDP-D-mannose 3 " ,5 " -epimerase is, to our knowledge, a novel member of the extended short-chain dehydrogenase/reductase family. The enzyme was cloned and expressed in Escherichia coli cells.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
BIOSYNTHESIS, PROTEIN, DEHYDROGENASE, MUR1 GENE, CELL-WALLS, ESCHERICHIA-COLI, L-FUCOSE, L-ASCORBIC-ACID, DE-NOVO SYNTHESIS, MULTIPLE SEQUENCE ALIGNMENT
journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Proc. Natl. Acad. Sci. USA
volume
98
issue
26
pages
14843 - 14848
Web of Science type
Article
Web of Science id
000172848800022
JCR category
MULTIDISCIPLINARY SCIENCES
JCR impact factor
10.896 (2001)
JCR rank
3/45 (2001)
JCR quartile
1 (2001)
ISSN
0027-8424
DOI
10.1073/pnas.011578198
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
138840
handle
http://hdl.handle.net/1854/LU-138840
date created
2004-01-14 13:37:00
date last changed
2016-12-19 15:37:50
@article{138840,
  abstract     = {The first step in the biosynthetic pathway of vitamin C in plants is the formation, at the level of sugar nucleotide, Of L-galactosyl residues, catalyzed by a largely unknown GDP-D-mannose 3 {\textacutedbl} ,5 {\textacutedbl} -epimerase. By using combined conventional biochemical and mass spectrometry methods, we obtained a highly purified preparation of GDP-D-mannose 3 {\textacutedbl} ,5 {\textacutedbl} -epimerase from an Arabidopsis thaliana cell suspension. The native enzyme is an 84-kDa dimer, composed of two apparently identical subunits. In-gel tryptic digestion of the enzyme subunit, followed by peptide sequencing and a BLAST search, led to the identification of the epimerase gene. The closest homolog of the plant epimerase is the BlmG gene product of Streptomyces sp., a putative NDP-D-mannose 5 {\textacutedbl} -epimerase. The plant GDP-D-mannose 3 {\textacutedbl} ,5 {\textacutedbl} -epimerase is, to our knowledge, a novel member of the extended short-chain dehydrogenase/reductase family. The enzyme was cloned and expressed in Escherichia coli cells.},
  author       = {Wolucka, Beata and Persiau, Geert and Van Doorsselaere, Jan and Davey, Mark W and Demol, Hans and Vandekerckhove, Jo{\"e}l and Van Montagu, Marc and Zabeau, Marc and Boerjan, Wout},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  keyword      = {BIOSYNTHESIS,PROTEIN,DEHYDROGENASE,MUR1 GENE,CELL-WALLS,ESCHERICHIA-COLI,L-FUCOSE,L-ASCORBIC-ACID,DE-NOVO SYNTHESIS,MULTIPLE SEQUENCE ALIGNMENT},
  language     = {eng},
  number       = {26},
  pages        = {14843--14848},
  title        = {Partial purification and identification of GDP-mannose 3{\textacutedbl}, 5{\textacutedbl}-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway},
  url          = {http://dx.doi.org/10.1073/pnas.011578198},
  volume       = {98},
  year         = {2001},
}

Chicago
Wolucka, Beata, Geert Persiau, Jan Van Doorsselaere, Mark W Davey, Hans Demol, Joël Vandekerckhove, Marc Van Montagu, Marc Zabeau, and Wout Boerjan. 2001. “Partial Purification and Identification of GDP-mannose 3‘, 5’-epimerase of Arabidopsis Thaliana, a Key Enzyme of the Plant Vitamin C Pathway.” Proceedings of the National Academy of Sciences of the United States of America 98 (26): 14843–14848.
APA
Wolucka, B., Persiau, G., Van Doorsselaere, J., Davey, M. W., Demol, H., Vandekerckhove, J., Van Montagu, M., et al. (2001). Partial purification and identification of GDP-mannose 3“, 5”-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 98(26), 14843–14848.
Vancouver
1.
Wolucka B, Persiau G, Van Doorsselaere J, Davey MW, Demol H, Vandekerckhove J, et al. Partial purification and identification of GDP-mannose 3“, 5”-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2001;98(26):14843–8.
MLA
Wolucka, Beata, Geert Persiau, Jan Van Doorsselaere, et al. “Partial Purification and Identification of GDP-mannose 3‘, 5’-epimerase of Arabidopsis Thaliana, a Key Enzyme of the Plant Vitamin C Pathway.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 98.26 (2001): 14843–14848. Print.