Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 76:40-44 (1984)
© 1984 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gumber, S. C.
Right arrow Articles by Loewus, F. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gumber, S. C.
Right arrow Articles by Loewus, F. A.
Agricola
Right arrow Articles by Gumber, S. C.
Right arrow Articles by Loewus, F. A.
Articles

Further Studies on myo-Inositol-1-phosphatase from the Pollen of Lilium longiflorum Thunb 1

Subhash C. Gumber, Mary W. Loewus and Frank A. Loewus

Program in Biochemistry/Biophysics and the Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340

myo-Inositol-1-phosphatase has been purified to homogeneity from Lilium longiflorum pollen using an alternative procedure which includes pH change and phenyl Sepharose column chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis shows that the enzyme is a dimer (subunit molecular weight, 29,000 daltons). The enzyme is stable at low pH values and is inactivated only below pH 3.0. In addition to 1L-and 1D-myo-inositol-1-phosphate, it shows high specificity for 1L-chiro-inositol-3-phosphate. As observed earlier with other primary phosphate esters, D-glucitol-6-phosphate and D-mannitol-6-phosphate are hydrolyzed very slowly. No activity is observed with inorganic pyrophosphate or myo-inositol pentaphosphate as substrate. The enzyme is inhibited by fluoride, sulfate, molybdate, and thiol-directed reagents. Partial protection against N-ethylmaleimide inhibition by substrate and Mg2+ together suggests sulfhydryl involvement at the active site.

1 Supported in part by Grant GM-22427 from the National Institute of Health, United States Public Health Service. Scientific Paper No. 6763, Project 0266, College of Agriculture Research Center, Washington State University, Pullman, WA 99164.




This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
W. A. Laing, S. Bulley, M. Wright, J. Cooney, D. Jensen, D. Barraclough, and E. MacRae
A highly specific L-galactose-1-phosphate phosphatase on the path to ascorbate biosynthesis
PNAS, November 30, 2004; 101(48): 16976 - 16981.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
L. Chen and M. F. Roberts
Characterization of a Tetrameric Inositol Monophosphatase from the Hyperthermophilic Bacterium Thermotoga maritima
Appl. Envir. Microbiol., October 1, 1999; 65(10): 4559 - 4567.
[Abstract] [Full Text]

Home page
 Appl. Environ. Microbiol.Home page
L. Chen and M. F. Roberts
Cloning and Expression of the Inositol Monophosphatase Gene from Methanococcus jannaschii and Characterization of the Enzyme
Appl. Envir. Microbiol., July 1, 1998; 64(7): 2609 - 2615.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
Z. Peng and D. P. S. Verma
A Rice HAL2-like Gene Encodes a Ca[IMAGE]-sensitive 3`(2`),5`-Diphosphonucleoside 3`(2`)-Phosphohydrolase and Complements Yeast met22 and Escherichia coli cysQ Mutations
J. Biol. Chem., December 8, 1995; 270(49): 29105 - 29110.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1984 by the American Society of Plant Biologists