R8000
D-Ribulose 1,5-Diphosphate Carboxylase from spinach
partially purified powder, 0.01-0.1 unit/mg solid
Synonym(s):
3-Phospho-D-glycerate carboxy-lyase(dimerizing), Rubisco
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
spinach
form
partially purified powder
specific activity
0.01-0.1 unit/mg solid
mol wt
557 kDa
storage temp.
−20°C
General description
D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) amounts to 50% of the total spinach leaves associated soluble protein.
Exists as a 557 kDa hexadecamer composed of eight heavy chains each with a molecular weight of approximately 56 kDa and eight light chains of molecular weight 14 kDa. Each molecule contains one magnesium ion.
pH optimum: ~7.9.
KM for CO2: ~0.45 mM.
Ribulose diphosphate becomes inhibitory at concentrations exceeding 0.7 mM. Orthophosphate and ammonium sulfate are competitive inhibitors. 3-Phosphoglycerate is a noncompetitive inhibitor.
pH optimum: ~7.9.
KM for CO2: ~0.45 mM.
Ribulose diphosphate becomes inhibitory at concentrations exceeding 0.7 mM. Orthophosphate and ammonium sulfate are competitive inhibitors. 3-Phosphoglycerate is a noncompetitive inhibitor.
Application
D-Ribulose 1,5-Diphosphate Carboxylase from spinach has been used:
- as a test protein in pepsin digestion studies
- as an innocuous or non-hazardous protein sample to test its effect on human intestinal epithelial cell lines
- in isothermal titration calorimetry (ITC), and radiolabeled binding assays with abscisic acid
Biochem/physiol Actions
D-Ribulose 1,5-Diphosphate Carboxylase (RUBISCO) depends on Rubisco activase and chaperones for activation. It participates in plant photorespiration events by catalyzing the carboxylation and oxygenation of ribulose-1,5-bisphosphate. Abscisic acid inhibits the carboxylation activity of Rubisco.
Unit Definition
One unit will convert 1.0 μmole of D-RuDP and CO2 to 2.0 μmoles of D-3-phosphoglycerate per min at pH 7.8 at 25°C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Guillaume Tcherkez
Plant, cell & environment, 36(9), 1586-1596 (2013-01-12)
Although ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) was discovered nearly 60 years ago, the associated chemical mechanism of the reaction is still incompletely understood. The catalytic cycle consists of four major steps: ribulose-1,5-bisphosphate binding, enolization, CO₂ or O₂ addition and hydration, and cleavage
Benjamin D Rae et al.
Microbiology and molecular biology reviews : MMBR, 77(3), 357-379 (2013-09-06)
Cyanobacteria are the globally dominant photoautotrophic lineage. Their success is dependent on a set of adaptations collectively termed the CO2-concentrating mechanism (CCM). The purpose of the CCM is to support effective CO2 fixation by enhancing the chemical conditions in the
Shunsuke Adachi et al.
Journal of experimental botany, 64(4), 1061-1072 (2013-01-26)
Increases in rates of individual leaf photosynthesis (P(n)) are critical for future increases in yields of rice plants. Although many efforts have been made to improve rice P(n) with transgenic technology, the desired increases in P(n) have not yet been
Inger Andersson
Journal of experimental botany, 59(7), 1555-1568 (2008-04-18)
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO(2) into the organic molecules of life. Rubisco is extremely inefficient as a catalyst and its carboxylase activity is compromised by numerous side-reactions including oxygenation of its sugar phosphate substrate by atmospheric
Jenna L Losh et al.
The New phytologist, 198(1), 52-58 (2013-01-25)
Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco) concentrations were quantified as a proportion of total protein in eight species of microalgae. This enzyme has been assumed to be a major fraction of total protein in phytoplankton, as has been demonstrated in
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