On the mechanism of fructose 1,6-diphosphatase: Inhibition by methyl d-fructoside 1,6-diphosphate

Stephen Benkovic, M. M. de Maine, J. J. Kleinschuster

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

From a comparison of the effects of potential inhibitors it is concluded that the furanose configuration of fructose 1,6-diphosphate is utilized by FDPase. The partial competitive inhibitor methyl d-fructoside 1,6-diphosphate, apparently induces a conformational change that permits acetylation of the active site. The probable importance of the C-2 hydroxyl of the sugar phosphate in the mechanism of FDPase is discussed.

Original languageEnglish (US)
Pages (from-to)248-251
Number of pages4
JournalArchives of Biochemistry and Biophysics
Volume139
Issue number1
DOIs
StatePublished - Jan 1 1970

Fingerprint

Fructose-Bisphosphatase
Diphosphates
Sugar Phosphates
Acetylation
Hydroxyl Radical
Catalytic Domain
fructose-1,6-diphosphate

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Benkovic, Stephen ; de Maine, M. M. ; Kleinschuster, J. J. / On the mechanism of fructose 1,6-diphosphatase : Inhibition by methyl d-fructoside 1,6-diphosphate. In: Archives of Biochemistry and Biophysics. 1970 ; Vol. 139, No. 1. pp. 248-251.
@article{9816f559a7fb4bdda5453eb2e3f52c9f,
title = "On the mechanism of fructose 1,6-diphosphatase: Inhibition by methyl d-fructoside 1,6-diphosphate",
abstract = "From a comparison of the effects of potential inhibitors it is concluded that the furanose configuration of fructose 1,6-diphosphate is utilized by FDPase. The partial competitive inhibitor methyl d-fructoside 1,6-diphosphate, apparently induces a conformational change that permits acetylation of the active site. The probable importance of the C-2 hydroxyl of the sugar phosphate in the mechanism of FDPase is discussed.",
author = "Stephen Benkovic and {de Maine}, {M. M.} and Kleinschuster, {J. J.}",
year = "1970",
month = "1",
day = "1",
doi = "10.1016/0003-9861(70)90068-8",
language = "English (US)",
volume = "139",
pages = "248--251",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

On the mechanism of fructose 1,6-diphosphatase : Inhibition by methyl d-fructoside 1,6-diphosphate. / Benkovic, Stephen; de Maine, M. M.; Kleinschuster, J. J.

In: Archives of Biochemistry and Biophysics, Vol. 139, No. 1, 01.01.1970, p. 248-251.

Research output: Contribution to journalArticle

TY - JOUR

T1 - On the mechanism of fructose 1,6-diphosphatase

T2 - Inhibition by methyl d-fructoside 1,6-diphosphate

AU - Benkovic, Stephen

AU - de Maine, M. M.

AU - Kleinschuster, J. J.

PY - 1970/1/1

Y1 - 1970/1/1

N2 - From a comparison of the effects of potential inhibitors it is concluded that the furanose configuration of fructose 1,6-diphosphate is utilized by FDPase. The partial competitive inhibitor methyl d-fructoside 1,6-diphosphate, apparently induces a conformational change that permits acetylation of the active site. The probable importance of the C-2 hydroxyl of the sugar phosphate in the mechanism of FDPase is discussed.

AB - From a comparison of the effects of potential inhibitors it is concluded that the furanose configuration of fructose 1,6-diphosphate is utilized by FDPase. The partial competitive inhibitor methyl d-fructoside 1,6-diphosphate, apparently induces a conformational change that permits acetylation of the active site. The probable importance of the C-2 hydroxyl of the sugar phosphate in the mechanism of FDPase is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0014813847&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014813847&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(70)90068-8

DO - 10.1016/0003-9861(70)90068-8

M3 - Article

C2 - 4320534

AN - SCOPUS:0014813847

VL - 139

SP - 248

EP - 251

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -