Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver

P. A. Benkovic; W. P. Bullard; M. de Maine; R. Fishbein; K. J. Schray; J. J. Steffens; S. J. Benkovic

Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver

P. A. Benkovic, W. P. Bullard, M. de Maine, R. Fishbein, K. J. Schray, J. J. Steffens, S. J. Benkovic

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

Abstract

The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P ₂. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.

Original language	English (US)
Pages (from-to)	930-931
Number of pages	2
Journal	Journal of Biological Chemistry
Volume	249
Issue number	3
State	Published - 1974

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

Cite this

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title = "Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver",

abstract = "The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P 2. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.",

author = "Benkovic, {P. A.} and Bullard, {W. P.} and {de Maine}, M. and R. Fishbein and Schray, {K. J.} and Steffens, {J. J.} and Benkovic, {S. J.}",

year = "1974",

language = "English (US)",

volume = "249",

pages = "930--931",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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T1 - Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver

AU - Benkovic, P. A.

AU - Bullard, W. P.

AU - de Maine, M.

AU - Fishbein, R.

AU - Schray, K. J.

AU - Steffens, J. J.

AU - Benkovic, S. J.

PY - 1974

Y1 - 1974

N2 - The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P 2. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.

AB - The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P 2. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.

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M3 - Article

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AN - SCOPUS:0015990306

SN - 0021-9258

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 3

ER -

Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver

Abstract

All Science Journal Classification (ASJC) codes

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