| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 265, Issue 19, 10817-10820, Jul, 1990
VA Reddy and F Maley
Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany.
Deglycosylated yeast invertase is irreversibly inactivated by conduritol B epoxide (CBE), an active-site-directed reagent. The inactivated enzyme contained 0.8 mol of CBE/mol of invertase monomer suggesting that the inactivation results from the modification of a single amino acid residue. Peptic digestion of [3H]CBE-labeled invertase followed by reverse phase column chromatography yielded two labeled peptides, both located at the amino-terminal end of the enzyme. Sequence analyses of these peptides revealed that Asp-23 is the modified residue. The role of Asp-23 in the catalytic process was investigated by changing it to Asn using site-directed mutagenesis of the SCU2 gene. The mutant enzyme was basically inactive, confirming a role for Asp-23 in the catalytic process.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Le Roy, W. Lammens, M. Verhaest, B. De Coninck, A. Rabijns, A. Van Laere, and W. Van den Ende Unraveling the Difference between Invertases and Fructan Exohydrolases: A Single Amino Acid (Asp-239) Substitution Transforms Arabidopsis Cell Wall Invertase1 into a Fructan 1-Exohydrolase Plant Physiology, November 1, 2007; 145(3): 616 - 625. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K.-Y. Kim, S. Rhee, and S.-I. Kim Role of the N-Terminal Domain of Endoinulinase from Arthrobacter sp. S37 in Regulation of Enzyme Catalysis J. Biochem., July 1, 2005; 138(1): 27 - 33. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Alberto, C. Bignon, G. Sulzenbacher, B. Henrissat, and M. Czjzek The Three-dimensional Structure of Invertase ({beta}-Fructosidase) from Thermotoga maritima Reveals a Bimodular Arrangement and an Evolutionary Relationship between Retaining and Inverting Glycosidases J. Biol. Chem., April 30, 2004; 279(18): 18903 - 18910. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. A. Gallagher, A. J. Cairns, and C. J. Pollock Cloning and characterization of a putative fructosyltransferase and two putative invertase genes from the temperate grass Lolium temulentum L. J. Exp. Bot., March 1, 2004; 55(397): 557 - 569. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Barrangou, E. Altermann, R. Hutkins, R. Cano, and T. R. Klaenhammer Functional and comparative genomic analyses of an operon involved in fructooligosaccharide utilization by Lactobacillus acidophilus PNAS, July 22, 2003; 100(15): 8957 - 8962. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. A. Burne, Z. T. Wen, Y.-Y. M. Chen, and J. E. C. Penders Regulation of Expression of the Fructan Hydrolase Gene of Streptococcus mutans GS-5 by Induction and Carbon Catabolite Repression J. Bacteriol., May 1, 1999; 181(9): 2863 - 2871. [Abstract] [Full Text]
|
|
|
|
|
|
A. Reddy and F. Maley Studies on Identifying the Catalytic Role of Glu-204 in the Active Site of Yeast Invertase J. Biol. Chem., June 14, 1996; 271(24): 13953 - 13958. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
