The role of tryptophan in neutral fructose diphosphatase

S. J. Benkovic; W. A. Frey; C. B. Libby; J. J. Villafranca

doi:10.1016/S0006-291X(74)80376-1

The role of tryptophan in neutral fructose diphosphatase

S. J. Benkovic, W. A. Frey, C. B. Libby, J. J. Villafranca

Chemistry

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Neutral rabbit liver fructose-1,6-diphosphatase which does not contain tryptophan has been isolated and shown to possess catalytic properties identical to that for the neutral enzyme which contains tryptophan. Criteria include pH activity optimum, EDTA and oleate activation, AMP inhibition and specific activity. However, the enzyme lacking tryptophan responds differently to proteolysis by subtilisin exhibiting a more rapid loss of sensitivity to AMP inhibition.

Original language	English (US)
Pages (from-to)	196-203
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	57
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(74)80376-1
State	Published - Mar 15 1974

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Neutral rabbit liver fructose-1,6-diphosphatase which does not contain tryptophan has been isolated and shown to possess catalytic properties identical to that for the neutral enzyme which contains tryptophan. Criteria include pH activity optimum, EDTA and oleate activation, AMP inhibition and specific activity. However, the enzyme lacking tryptophan responds differently to proteolysis by subtilisin exhibiting a more rapid loss of sensitivity to AMP inhibition.",

author = "Benkovic, {S. J.} and Frey, {W. A.} and Libby, {C. B.} and Villafranca, {J. J.}",

note = "Funding Information: This work was supported by a grant from the National Institute of Health, GM-13306 (SJB), and an appropriation from the Pennsylvania State University.",

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AU - Frey, W. A.

AU - Libby, C. B.

AU - Villafranca, J. J.

N1 - Funding Information: This work was supported by a grant from the National Institute of Health, GM-13306 (SJB), and an appropriation from the Pennsylvania State University.

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N2 - Neutral rabbit liver fructose-1,6-diphosphatase which does not contain tryptophan has been isolated and shown to possess catalytic properties identical to that for the neutral enzyme which contains tryptophan. Criteria include pH activity optimum, EDTA and oleate activation, AMP inhibition and specific activity. However, the enzyme lacking tryptophan responds differently to proteolysis by subtilisin exhibiting a more rapid loss of sensitivity to AMP inhibition.

AB - Neutral rabbit liver fructose-1,6-diphosphatase which does not contain tryptophan has been isolated and shown to possess catalytic properties identical to that for the neutral enzyme which contains tryptophan. Criteria include pH activity optimum, EDTA and oleate activation, AMP inhibition and specific activity. However, the enzyme lacking tryptophan responds differently to proteolysis by subtilisin exhibiting a more rapid loss of sensitivity to AMP inhibition.

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The role of tryptophan in neutral fructose diphosphatase

Abstract

All Science Journal Classification (ASJC) codes

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