Literature DB >> 6466304

Inactive forms of wheat ribulose bisphosphate carboxylase. Conversion from the slowly activating into the rapidly activating form.

C N Schmidt, S Gutteridge, M A Parry, A J Keys.   

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.

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Year:  1984        PMID: 6466304      PMCID: PMC1153696          DOI: 10.1042/bj2200781

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  17 in total

1.  Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.

Authors:  K Shinozaki; C Yamada; N Takahata; M Sugiura
Journal:  Proc Natl Acad Sci U S A       Date:  1983-07       Impact factor: 11.205

2.  Ribulose diphosphate carboxylase/oxygenase. IV. Regulation by phosphate esters.

Authors:  F J Ryan; N E Tolbert
Journal:  J Biol Chem       Date:  1975-06-10       Impact factor: 5.157

3.  Structural patterns in globular proteins.

Authors:  M Levitt; C Chothia
Journal:  Nature       Date:  1976-06-17       Impact factor: 49.962

4.  Identification of two binding sites of the D-ribulose 1,5-bisphosphate carboxylase/oxygenase from spinach for D-ribulose 1,5-bisphosphate and effectors of the carboxylation reaction.

Authors:  J Vater; J Salnikow
Journal:  Arch Biochem Biophys       Date:  1979-04-15       Impact factor: 4.013

5.  The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA.

Authors:  G Zurawski; B Perrot; W Bottomley; P R Whitfeld
Journal:  Nucleic Acids Res       Date:  1981-07-24       Impact factor: 16.971

6.  On the mechanism of effector-mediated activation of ribulose bisphosphate carboxylase/oxygenase.

Authors:  S D McCurry; J Pierce; N E Tolbert; W H Orme-Johnson
Journal:  J Biol Chem       Date:  1981-07-10       Impact factor: 5.157

7.  A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase.

Authors:  W A Laing; J T Christeller
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

8.  A kinetic study of ribulose bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum.

Authors:  J T Christeller; W A Laing
Journal:  Biochem J       Date:  1978-08-01       Impact factor: 3.857

9.  Regulation of ribulose 1,5-diphosphate carboxylase by substrates and other metabolites: further evidence for several types of binding sites.

Authors:  D K Chu; J A Bassham
Journal:  Plant Physiol       Date:  1975-04       Impact factor: 8.340

10.  Carbamate formation on the epsilon-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+.

Authors:  G H Lorimer; H M Miziorko
Journal:  Biochemistry       Date:  1980-11-11       Impact factor: 3.162

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  2 in total

1.  A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding.

Authors:  C A Kettleborough; A L Phillips; A J Keys; M A Parry
Journal:  Planta       Date:  1991-04       Impact factor: 4.116

2.  Rubisco activity: effects of drought stress.

Authors:  Martin A J Parry; P John Andralojc; Shahnaz Khan; Peter J Lea; Alfred J Keys
Journal:  Ann Bot       Date:  2002-06       Impact factor: 4.357

  2 in total

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