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
Quality Level
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
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Dennis McNevin et al.
Journal of experimental botany, 57(14), 3883-3900 (2006-10-19)
The forward and reverse rate constants involved in carbamylation, activation, carboxylation, and inhibition of D-ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) have been estimated by a new technique of simultaneous non-linear regression of a differential equation kinetic model to multiple experimental data. Parameters predicted
K Thomas et al.
Regulatory toxicology and pharmacology : RTP, 39(2), 87-98 (2004-03-26)
Rationale. Evaluation of the potential allergenicity of proteins derived from genetically modified foods has involved a weight of evidence approach that incorporates an evaluation of protein digestibility in pepsin. Currently, there is no standardized protocol to assess the digestibility of
Martin A J Parry et al.
Journal of experimental botany, 64(3), 717-730 (2012-11-20)
Rubisco (ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase) enables net carbon fixation through the carboxylation of RuBP. However, some characteristics of Rubisco make it surprisingly inefficient and compromise photosynthetic productivity. For example, Rubisco catalyses a wasteful reaction with oxygen that leads to the release
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
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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