Kinetic hysteresis for fructose bisphosphatase: A change in substrate configuration specificity

M. M. deMaine, S. J. Benkovic

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Kinetic hysteresis for rabbit liver fructose bisphosphatase in the presence of Mg2+ (pH 7.6) is exhibited by the varied rates at which product formation is reduced on the addition of different inhibitors under cycling conditions. Two different states of the enzyme are detected: the initial resting state which binds α-, β- and keto analogs of fructose 1,6-bisphosphate; and the active cycling state which binds, and is inhibited by, only the α-analog. Both enzyme states, however, bind the allosteric modifier, AMP, and a product analog, (α+β)methyl-D-fructofuranoside 6-phosphate to the same extent so that the resulting inhibition is state independent. A relatively slow first-order transition (0.13 min-1) characterizes the reversion of the active enzyme to its resting state. The implications of this phenomenon for regulating fructose bisphosphatase activity in vivo are discussed.

Original languageEnglish (US)
Pages (from-to)835-840
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume88
Issue number3
DOIs
StatePublished - Jun 13 1979

Fingerprint

Fructose-Bisphosphatase
Substrate Specificity
Hysteresis
Kinetics
Substrates
Enzymes
Adenosine Monophosphate
Liver
Phosphates
Rabbits

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{32b44b1cc8844c2c807c180a855924bc,
title = "Kinetic hysteresis for fructose bisphosphatase: A change in substrate configuration specificity",
abstract = "Kinetic hysteresis for rabbit liver fructose bisphosphatase in the presence of Mg2+ (pH 7.6) is exhibited by the varied rates at which product formation is reduced on the addition of different inhibitors under cycling conditions. Two different states of the enzyme are detected: the initial resting state which binds α-, β- and keto analogs of fructose 1,6-bisphosphate; and the active cycling state which binds, and is inhibited by, only the α-analog. Both enzyme states, however, bind the allosteric modifier, AMP, and a product analog, (α+β)methyl-D-fructofuranoside 6-phosphate to the same extent so that the resulting inhibition is state independent. A relatively slow first-order transition (0.13 min-1) characterizes the reversion of the active enzyme to its resting state. The implications of this phenomenon for regulating fructose bisphosphatase activity in vivo are discussed.",
author = "deMaine, {M. M.} and Benkovic, {S. J.}",
year = "1979",
month = "6",
day = "13",
doi = "10.1016/0006-291X(79)91484-0",
language = "English (US)",
volume = "88",
pages = "835--840",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

Kinetic hysteresis for fructose bisphosphatase : A change in substrate configuration specificity. / deMaine, M. M.; Benkovic, S. J.

In: Biochemical and Biophysical Research Communications, Vol. 88, No. 3, 13.06.1979, p. 835-840.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Kinetic hysteresis for fructose bisphosphatase

T2 - A change in substrate configuration specificity

AU - deMaine, M. M.

AU - Benkovic, S. J.

PY - 1979/6/13

Y1 - 1979/6/13

N2 - Kinetic hysteresis for rabbit liver fructose bisphosphatase in the presence of Mg2+ (pH 7.6) is exhibited by the varied rates at which product formation is reduced on the addition of different inhibitors under cycling conditions. Two different states of the enzyme are detected: the initial resting state which binds α-, β- and keto analogs of fructose 1,6-bisphosphate; and the active cycling state which binds, and is inhibited by, only the α-analog. Both enzyme states, however, bind the allosteric modifier, AMP, and a product analog, (α+β)methyl-D-fructofuranoside 6-phosphate to the same extent so that the resulting inhibition is state independent. A relatively slow first-order transition (0.13 min-1) characterizes the reversion of the active enzyme to its resting state. The implications of this phenomenon for regulating fructose bisphosphatase activity in vivo are discussed.

AB - Kinetic hysteresis for rabbit liver fructose bisphosphatase in the presence of Mg2+ (pH 7.6) is exhibited by the varied rates at which product formation is reduced on the addition of different inhibitors under cycling conditions. Two different states of the enzyme are detected: the initial resting state which binds α-, β- and keto analogs of fructose 1,6-bisphosphate; and the active cycling state which binds, and is inhibited by, only the α-analog. Both enzyme states, however, bind the allosteric modifier, AMP, and a product analog, (α+β)methyl-D-fructofuranoside 6-phosphate to the same extent so that the resulting inhibition is state independent. A relatively slow first-order transition (0.13 min-1) characterizes the reversion of the active enzyme to its resting state. The implications of this phenomenon for regulating fructose bisphosphatase activity in vivo are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0018789353&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018789353&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(79)91484-0

DO - 10.1016/0006-291X(79)91484-0

M3 - Article

C2 - 223573

AN - SCOPUS:0018789353

VL - 88

SP - 835

EP - 840

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -