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Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme. / Parry, Martin A. J.; Schmidt, C. N. Godfrey; Cornelius, Martin J. et al.
In: Journal of Experimental Botany, Vol. 36, No. 9, 09.1985, p. 1396-1404.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Parry, MAJ, Schmidt, CNG, Cornelius, MJ, Keys, AJ & Millard, BN 1985, 'Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme', Journal of Experimental Botany, vol. 36, no. 9, pp. 1396-1404. https://doi.org/10.1093/jxb/36.9.1396

APA

Parry, M. A. J., Schmidt, C. N. G., Cornelius, M. J., Keys, A. J., & Millard, B. N. (1985). Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme. Journal of Experimental Botany, 36(9), 1396-1404. https://doi.org/10.1093/jxb/36.9.1396

Vancouver

Parry MAJ, Schmidt CNG, Cornelius MJ, Keys AJ, Millard BN. Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme. Journal of Experimental Botany. 1985 Sept;36(9):1396-1404. doi: 10.1093/jxb/36.9.1396

Author

Parry, Martin A. J. ; Schmidt, C. N. Godfrey ; Cornelius, Martin J. et al. / Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2 : co-operativity between the subunits of the enzyme. In: Journal of Experimental Botany. 1985 ; Vol. 36, No. 9. pp. 1396-1404.

Bibtex

@article{acb63bb2815b4b3abcc26a0e57f21ba7,
title = "Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2: co-operativity between the subunits of the enzyme",
abstract = "Ribulose bisphosphate carboxylase/oxygenase (E.C. 4.1.1.39) from wheat (Triticum aestivum L.), already activated by reaction with CO2 and Mg2+, was increased in activity on addition of inorganic orthophosphate. This further activation took place without a significant increase in the amount of bound activating CO2 and the effect was relatively greater with smaller amounts of bound CO2. With less than 2·0 mol of CO2 bound per mol holoenzyme, phosphate increased activity about five-fold whilst with 7·0 mol of bound activating CO2 per mol holoenzyme, phosphate increased activity by a factor of only 1 ·8. This decrease in the effect of orthophosphate with increase in bound activating CO2 suggests negative co-operativity between activated sites. The stimulation of activity by inorganic orthophosphate must be a process distinct from activation by CO2; it was observed with both the slow and the rapidly activating forms of ribulose bisphosphate carboxylase/oxygenase from wheat. ",
keywords = "Activation, Co-operativity, Inorganic orthophosphate CO2, Ribulose bisphosphate carboxylase",
author = "Parry, {Martin A. J.} and Schmidt, {C. N. Godfrey} and Cornelius, {Martin J.} and Keys, {Alfred J.} and Millard, {Barbara N.}",
year = "1985",
month = sep,
doi = "10.1093/jxb/36.9.1396",
language = "English",
volume = "36",
pages = "1396--1404",
journal = "Journal of Experimental Botany",
issn = "0022-0957",
publisher = "OXFORD UNIV PRESS",
number = "9",

}

RIS

TY - JOUR

T1 - Stimulation of ribulose bisphosphate carboxylase activity by inorganic orthophosphate without an increase in bound activating CO2

T2 - co-operativity between the subunits of the enzyme

AU - Parry, Martin A. J.

AU - Schmidt, C. N. Godfrey

AU - Cornelius, Martin J.

AU - Keys, Alfred J.

AU - Millard, Barbara N.

PY - 1985/9

Y1 - 1985/9

N2 - Ribulose bisphosphate carboxylase/oxygenase (E.C. 4.1.1.39) from wheat (Triticum aestivum L.), already activated by reaction with CO2 and Mg2+, was increased in activity on addition of inorganic orthophosphate. This further activation took place without a significant increase in the amount of bound activating CO2 and the effect was relatively greater with smaller amounts of bound CO2. With less than 2·0 mol of CO2 bound per mol holoenzyme, phosphate increased activity about five-fold whilst with 7·0 mol of bound activating CO2 per mol holoenzyme, phosphate increased activity by a factor of only 1 ·8. This decrease in the effect of orthophosphate with increase in bound activating CO2 suggests negative co-operativity between activated sites. The stimulation of activity by inorganic orthophosphate must be a process distinct from activation by CO2; it was observed with both the slow and the rapidly activating forms of ribulose bisphosphate carboxylase/oxygenase from wheat.

AB - Ribulose bisphosphate carboxylase/oxygenase (E.C. 4.1.1.39) from wheat (Triticum aestivum L.), already activated by reaction with CO2 and Mg2+, was increased in activity on addition of inorganic orthophosphate. This further activation took place without a significant increase in the amount of bound activating CO2 and the effect was relatively greater with smaller amounts of bound CO2. With less than 2·0 mol of CO2 bound per mol holoenzyme, phosphate increased activity about five-fold whilst with 7·0 mol of bound activating CO2 per mol holoenzyme, phosphate increased activity by a factor of only 1 ·8. This decrease in the effect of orthophosphate with increase in bound activating CO2 suggests negative co-operativity between activated sites. The stimulation of activity by inorganic orthophosphate must be a process distinct from activation by CO2; it was observed with both the slow and the rapidly activating forms of ribulose bisphosphate carboxylase/oxygenase from wheat.

KW - Activation

KW - Co-operativity

KW - Inorganic orthophosphate CO2

KW - Ribulose bisphosphate carboxylase

U2 - 10.1093/jxb/36.9.1396

DO - 10.1093/jxb/36.9.1396

M3 - Journal article

AN - SCOPUS:0001646729

VL - 36

SP - 1396

EP - 1404

JO - Journal of Experimental Botany

JF - Journal of Experimental Botany

SN - 0022-0957

IS - 9

ER -