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.",

number = "3",

}

TY - JOUR

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.

UR - https://www.scopus.com/pages/publications/0015990306

UR - https://www.scopus.com/pages/publications/0015990306#tab=citedBy

M3 - Article

C2 - 4359777

AN - SCOPUS:0015990306

SN - 0021-9258

VL - 249

SP - 930

EP - 931

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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