5 Ribulose-1,5-Diphosphate Carboxylase

Siegel, Marvín I.; Wishnick, Marcia; Lane, M. Daniel

doi:10.1016/s1874-6047(08)60040-2

Cited by 32 publications

(16 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although RuDPCase has been known for 20 years and has been extensively studied and its properties reviewed (12,15,24), the specific type of allosteric behavior described in this and our two previous reports (10,11) has largely escaped notice. Probably this is due to the fact that, although Pon et al.…”

Section: Discussionmentioning

confidence: 76%

Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites

Chu¹,

Bassham²

1975

Plant Physiol.

View full text Add to dashboard Cite

Ribulose 1, 5-diphosphate carboxylase (RuDPCase, EC 4.1.1.39) isolated from spinach leaves is metabolically regulated at 10 mM Mg2+ and low C02 concentrations by its substrates (RuDP and C02) and by effectors which include 6-phosphogluconate (6-PGluA), NADPH, and fructose 1,6-diphosphate (FDP), but not fructose '6-phosphate. Physiological concentrations of RuDP severely inhibit the enzyme activity when the enzyme has not been preincubated with HCO3-and Mg2-, and this inactivity persists for 20 minutes or longer after 1 mM HCO,-and 10 mM Mg2+ are added. Maximum activity requires that the preincubation mixture also include either 0.01 mm 6-PGluA or 0.5 mM NADPH.When the enzyme, following preincubation with HC03-and Mg2+, is presented with RuDP plus either 6-PGluA or FDP, competitive inhibition is observed with respect to RuDP.

show abstract

Section: Discussionmentioning

confidence: 76%

Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites

Chu¹,

Bassham²

1975

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…Immunochemical and SH-reagent experiments have identified the large subunit of the protein as the site of both reactions (78,102). Cyanide and 2-carboxyribitol I,S-bisphosphate inhibit the oxygenase (70, 91) as well as the carboxylase (92,93). Since the oxygenase and carboxylase are activated in like manner on the same protein, it appears quite likely that the same active site is involved in both reactions (10, 6S).…”

Section: Oxygenase Activitymentioning

confidence: 99%

Ribulose 1,5-Bisphosphate Carboxylase-Oxygenase

Jensen¹,

Bahr²

1977

Annu. Rev. Plant. Physiol.

393

161

View full text Add to dashboard Cite

“…Studies, reviewed by Kawashima & Wildman (1970a) and Siegel et al (1972), have defined several physical properties of the enzyme. The sedimentation coefficient, of RuDPCase † from various plant sources has an average value of 18·5 S. The molecular weight, determined from sedimentation velocity and diffusion experiments, and from sedimentation equilibrium, has values ranging from 480,000 to 590,000.…”

Section: Introductionmentioning

confidence: 99%

The structure of form I crystals of d-ribulose-1,5-diphosphate carboxylase

Baker

Eisenberg

Eiserling

et al. 1975

Journal of Molecular Biology

109

View full text Add to dashboard Cite

Single crystals of D-ribulose-1,5-diphosphate carboxylase from tobacco leaves, Nicotiana tabacum (variety Turkish Samsun), have been examined by X-ray diffraction, electron microscopy, and optical diffraction. Twelve molecules are loosely packed into a body-centered cubic unit cell, space group 14 1 32 with cell dimension a = 383 Å. The asymmetric unit is one quarter of a molecule, and the minimum molecular symmetry is 222. This symmetry when combined with estimates of the two subunit masses and stoichiometry is compatible with a molecular structure of the composition L 8 S 8 (L is large subunit, S is small). If all bonds between large and small subunits are equivalent, the true molecular symmetry is 422; this symmetry is consistent with molecular images in micrographs.

show abstract

5 Ribulose-1,5-Diphosphate Carboxylase

Cited by 32 publications

References 76 publications

Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites

Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites

Ribulose 1,5-Bisphosphate Carboxylase-Oxygenase

The structure of form I crystals of d-ribulose-1,5-diphosphate carboxylase

Contact Info

Product

Resources

About