Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity.

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Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity. / Krath, B N; Hove-Jensen, B.

In: Journal of Biological Chemistry, Vol. 276, No. 21, 2001, p. 17851-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Krath, BN & Hove-Jensen, B 2001, 'Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity.', Journal of Biological Chemistry, vol. 276, no. 21, pp. 17851-6. https://doi.org/10.1074/jbc.M010172200

APA

Krath, B. N., & Hove-Jensen, B. (2001). Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity. Journal of Biological Chemistry, 276(21), 17851-6. https://doi.org/10.1074/jbc.M010172200

Vancouver

Krath BN, Hove-Jensen B. Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity. Journal of Biological Chemistry. 2001;276(21):17851-6. https://doi.org/10.1074/jbc.M010172200

Author

Krath, B N ; Hove-Jensen, B. / Class II recombinant phosphoribosyl diphosphate synthase from spinach. Phosphate independence and diphosphoryl donor specificity. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 21. pp. 17851-6.

Bibtex

@article{d8e92510ac1d11ddb5e9000ea68e967b,
title = "Class II recombinant phosphoribosyl diphosphate synthase from spinach.: Phosphate independence and diphosphoryl donor specificity.",
abstract = "A recombinant form of spinach (Spinacia oleracea) phosphoribosyl diphosphate (PRPP) synthase isozyme 3 resembling the presumed mature enzyme has been synthesized in an Escherichia coli strain in which the endogenous PRPP synthase gene was deleted, and has been purified to near homogeneity. Contrary to other PRPP synthases the activity of spinach PRPP synthase isozyme 3 is independent of P(i), and the enzyme is inhibited by ribonucleoside diphosphates in a purely competitive manner, which indicates a lack of allosteric inhibition by these compounds. In addition spinach PRPP synthase isozyme 3 shows an unusual low specificity toward diphosphoryl donors by accepting dATP, GTP, CTP, and UTP in addition to ATP. The kinetic mechanism of the enzyme is an ordered steady state Bi Bi mechanism with K(ATP) and K(Rib-5-P) values of 170 and 110 micrometer, respectively, and a V(max) value of 13.1 micromol (min x mg of protein)(-1). The enzyme has an absolute requirement for magnesium ions, and maximal activity is obtained at 40 degrees C at pH 7.6.",
author = "Krath, {B N} and B Hove-Jensen",
note = "Keywords: Catalysis; Isoenzymes; Kinetics; Recombinant Proteins; Ribose-Phosphate Pyrophosphokinase; Spinacia oleracea; Substrate Specificity",
year = "2001",
doi = "10.1074/jbc.M010172200",
language = "English",
volume = "276",
pages = "17851--6",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "21",

}

RIS

TY - JOUR

T1 - Class II recombinant phosphoribosyl diphosphate synthase from spinach.

T2 - Phosphate independence and diphosphoryl donor specificity.

AU - Krath, B N

AU - Hove-Jensen, B

N1 - Keywords: Catalysis; Isoenzymes; Kinetics; Recombinant Proteins; Ribose-Phosphate Pyrophosphokinase; Spinacia oleracea; Substrate Specificity

PY - 2001

Y1 - 2001

N2 - A recombinant form of spinach (Spinacia oleracea) phosphoribosyl diphosphate (PRPP) synthase isozyme 3 resembling the presumed mature enzyme has been synthesized in an Escherichia coli strain in which the endogenous PRPP synthase gene was deleted, and has been purified to near homogeneity. Contrary to other PRPP synthases the activity of spinach PRPP synthase isozyme 3 is independent of P(i), and the enzyme is inhibited by ribonucleoside diphosphates in a purely competitive manner, which indicates a lack of allosteric inhibition by these compounds. In addition spinach PRPP synthase isozyme 3 shows an unusual low specificity toward diphosphoryl donors by accepting dATP, GTP, CTP, and UTP in addition to ATP. The kinetic mechanism of the enzyme is an ordered steady state Bi Bi mechanism with K(ATP) and K(Rib-5-P) values of 170 and 110 micrometer, respectively, and a V(max) value of 13.1 micromol (min x mg of protein)(-1). The enzyme has an absolute requirement for magnesium ions, and maximal activity is obtained at 40 degrees C at pH 7.6.

AB - A recombinant form of spinach (Spinacia oleracea) phosphoribosyl diphosphate (PRPP) synthase isozyme 3 resembling the presumed mature enzyme has been synthesized in an Escherichia coli strain in which the endogenous PRPP synthase gene was deleted, and has been purified to near homogeneity. Contrary to other PRPP synthases the activity of spinach PRPP synthase isozyme 3 is independent of P(i), and the enzyme is inhibited by ribonucleoside diphosphates in a purely competitive manner, which indicates a lack of allosteric inhibition by these compounds. In addition spinach PRPP synthase isozyme 3 shows an unusual low specificity toward diphosphoryl donors by accepting dATP, GTP, CTP, and UTP in addition to ATP. The kinetic mechanism of the enzyme is an ordered steady state Bi Bi mechanism with K(ATP) and K(Rib-5-P) values of 170 and 110 micrometer, respectively, and a V(max) value of 13.1 micromol (min x mg of protein)(-1). The enzyme has an absolute requirement for magnesium ions, and maximal activity is obtained at 40 degrees C at pH 7.6.

U2 - 10.1074/jbc.M010172200

DO - 10.1074/jbc.M010172200

M3 - Journal article

C2 - 11278632

VL - 276

SP - 17851

EP - 17856

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -

ID: 8443929