小麦核酮糖二磷酸羧化酶的无活性形式。从缓慢激活形式向快速激活形式的转变。
Inactive forms of wheat ribulose bisphosphate carboxylase. Conversion from the slowly activating into the rapidly activating form.
作者信息
Schmidt C N, Gutteridge S, Parry M A, Keys A J
出版信息
Biochem J. 1984 Jun 15;220(3):781-5. doi: 10.1042/bj2200781.
Abstract
Wheat ribulose bisphosphate carboxylase can be converted from the slowly activating into the rapidly activating form by heat or effectors in the absence of CO2 and Mg2+. This conversion process had the same energy of activation of 95.6kJ/mol both in the presence and in the absence of effectors, whereas the free-energy change value ranged from +2.5kJ/mol to -3.4kJ/mol depending on the end product involved. Far-u.v. c.d. spectra measured before and after conversion indicated that ribulose bisphosphate carboxylase is an alpha/beta-class protein and that no significant changes in gross conformation occur. Signals in the near-u.v. region suggested that the main change during conversion is re-orientation of aromatic side chains, probably near the active site; a possible site for effector binding is discussed.
摘要
在没有二氧化碳和镁离子的情况下，小麦核酮糖二磷酸羧化酶可通过加热或效应物从缓慢激活形式转变为快速激活形式。无论有无效应物，这种转变过程的活化能均为95.6kJ/mol，而自由能变化值则根据所涉及的终产物在+2.5kJ/mol至-3.4kJ/mol之间变化。转变前后测得的远紫外圆二色光谱表明，核酮糖二磷酸羧化酶是一种α/β类蛋白质，其总体构象没有显著变化。近紫外区域的信号表明，转变过程中的主要变化是芳香族侧链的重新定向，可能靠近活性位点；文中还讨论了效应物结合的一个可能位点。
相似文献
1
Inactive forms of wheat ribulose bisphosphate carboxylase. Conversion from the slowly activating into the rapidly activating form.小麦核酮糖二磷酸羧化酶的无活性形式。从缓慢激活形式向快速激活形式的转变。
Biochem J. 1984 Jun 15;220(3):781-5. doi: 10.1042/bj2200781.
2
The reactions between active and inactive forms of wheat ribulosebisphosphate carboxylase and effectors.小麦核酮糖二磷酸羧化酶活性与非活性形式之间的反应及效应物
Eur J Biochem. 1982 Sep 1;126(3):597-602. doi: 10.1111/j.1432-1033.1982.tb06822.x.
3
Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase.磷酸糖与核酮糖-1,5-二磷酸羧化酶催化位点的相互作用。
Biochemistry. 1981 Apr 14;20(8):2219-25. doi: 10.1021/bi00511a023.
4
A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase.1,5-二磷酸核酮糖羧化酶激活与催化动力学模型
Biochem J. 1976 Dec 1;159(3):563-70. doi: 10.1042/bj1590563.
5
Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.菠菜1,5-二磷酸核酮糖羧化酶/加氧酶产物复合物的结构
Biochemistry. 1997 Apr 1;36(13):4041-6. doi: 10.1021/bi962818w.
6
A kinetic study of ribulose bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum.光合细菌红螺菌中二磷酸核酮糖羧化酶的动力学研究。
Biochem J. 1978 Aug 1;173(2):467-73. doi: 10.1042/bj1730467.
7
Inhibition and stimulation of ribulose-1,5-bisphosphate carboxylase/oxygenase by glyoxylate.乙醛酸对1,5-二磷酸核酮糖羧化酶/加氧酶的抑制与刺激作用
Arch Biochem Biophys. 1985 Jul;240(1):392-401. doi: 10.1016/0003-9861(85)90044-x.
8
Studies of the Co2+-activated ribulose-1,5-bisphosphate carboxylase/oxygenase by the use of spectrophotometry.利用分光光度法对二氧化碳激活的核酮糖-1,5-二磷酸羧化酶/加氧酶的研究。
Biochim Biophys Acta. 1989 Mar 16;995(1):75-81. doi: 10.1016/0167-4838(89)90236-7.
9
Effects of metabolite binding to ribulosebisphosphate carboxylase on the activity of the Calvin photosynthesis cycle.代谢物与核酮糖二磷酸羧化酶结合对卡尔文光合循环活性的影响。
Eur J Biochem. 1988 Nov 1;177(2):351-5. doi: 10.1111/j.1432-1033.1988.tb14382.x.
10
The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications.二氧化碳和镁离子对1,5-二磷酸核酮糖羧化酶的激活作用。平衡、动力学、一种推测的机制及生理意义。
Biochemistry. 1976 Feb 10;15(3):529-36. doi: 10.1021/bi00648a012.
引用本文的文献
1
A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding.一个位于核酮糖-1,5-二磷酸羧化酶 N 端的点突变影响核酮糖-1,5-二磷酸的结合。
Planta. 1991 Apr;184(1):35-9. doi: 10.1007/BF00208233.
2
Rubisco activity: effects of drought stress.核酮糖-1,5-二磷酸羧化酶/加氧酶活性：干旱胁迫的影响
Ann Bot. 2002 Jun;89 Spec No(7):833-9. doi: 10.1093/aob/mcf103.
本文引用的文献
1
Regulation of ribulose 1,5-diphosphate carboxylase by substrates and other metabolites: further evidence for several types of binding sites.1,5-二磷酸核酮糖羧化酶受底物及其他代谢物的调控：关于多种结合位点的进一步证据
Plant Physiol. 1975 Apr;55(4):720-6. doi: 10.1104/pp.55.4.720.
2
Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.藻蓝细菌核酮糖-1,5-二磷酸羧化酶/加氧酶大亚基基因的分子克隆和序列分析。
Proc Natl Acad Sci U S A. 1983 Jul;80(13):4050-4. doi: 10.1073/pnas.80.13.4050.
3
Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase.磷酸糖与核酮糖-1,5-二磷酸羧化酶催化位点的相互作用。
Biochemistry. 1981 Apr 14;20(8):2219-25. doi: 10.1021/bi00511a023.
4
The reactions between active and inactive forms of wheat ribulosebisphosphate carboxylase and effectors.小麦核酮糖二磷酸羧化酶活性与非活性形式之间的反应及效应物
Eur J Biochem. 1982 Sep 1;126(3):597-602. doi: 10.1111/j.1432-1033.1982.tb06822.x.
5
On the mechanism of effector-mediated activation of ribulose bisphosphate carboxylase/oxygenase.关于效应物介导的1,5-二磷酸核酮糖羧化酶/加氧酶激活机制
J Biol Chem. 1981 Jul 10;256(13):6623-8.
6
Carbamate formation on the epsilon-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+.赖氨酰残基的ε-氨基上形成氨基甲酸酯作为二氧化碳和镁离子激活核酮糖-1,5-二磷酸羧化酶的基础。
Biochemistry. 1980 Nov 11;19(23):5321-8. doi: 10.1021/bi00564a027.
7
The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA.菠菜叶绿体DNA中1,5-二磷酸核酮糖羧化酶大亚基的基因结构。
Nucleic Acids Res. 1981 Jul 24;9(14):3251-70. doi: 10.1093/nar/9.14.3251.
8
Regulation of ribulose 1,5-diphosphate carboxylase in the photosynthetic assimilation of carbon dioxide.光合作用中二氧化碳同化过程中1,5-二磷酸核酮糖羧化酶的调节
J Biol Chem. 1973 Jul 25;248(14):4956-64.
9
Regulation of ribulose 1,5-bisphosphate carboxylase-oxygenase activities by temperature pretreatment and chloroplast metabolites.通过温度预处理和叶绿体代谢产物对1,5-二磷酸核酮糖羧化酶加氧酶活性的调控
Arch Biochem Biophys. 1976 Sep;176(1):344-51. doi: 10.1016/0003-9861(76)90173-9.
10
Structural patterns in globular proteins.球状蛋白质中的结构模式。
Nature. 1976 Jun 17;261(5561):552-8. doi: 10.1038/261552a0.
Zotero 插件