Ribulose 1,5-bisphosphate carboxylase/oxygenase
Ribulose 1,5-diphosphate carboxylase/oxygenase
Ribulose bisphosphate carboxylase/oxygenase
Ribulose diphosphate carboxylase/oxygenase
For the enzyme, Rubisco, there are at least two different types of subunits: Catalytic large subunits and small subunits (see [30] & [31]). Molecular forms of Rubisco are determined by the presence or absence of the small subunits ([30] & [31]). The most common form (form I) is composed of large and small subunits, in a hexadecameric structure, L8S8 ([30] & [31]). The form II is a dimer of large subunits, (L2)n, and lacks small subunits ([30] and [31]). The form II comprises L2, L8 and L10, also lacking small subunits ([30] & [31]). Currently, this entry comprises the form II and form III, both of which lack small subunits. This enzyme catalyzes the incorporation of atmospheric CO2 into the organic molecule, ribulose-1,5-bisphosphate (RuBP) (carboxylation). However, this enzyme catalyzes several side-reactions, including oxygenation of RuBP by atmospheric O2, which compromise the carboxylation activity (see [23], [30] & [31]). The carboxylation: D-ribulose 1,5-bisphosphate + CO(2) + H(2)O = 2 3-phospho-D-glycerate + 2 H(+) The oxygenation: D-ribulose 1,5-bisphosphate + O(2) = 3-phospho-D-glycerate + 2-phosphoglycolate
The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain.
Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes.
Role of asparagine-111 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as explored by site-directed mutagenesis.
Chemical and genetic probes of the active site of D-ribulose-1,5-bisphosphate carboxylase/oxygenase: a retrospective based on the three-dimensional structure.
Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.
The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.
Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase.
Oxygenation mechanism of ribulose-bisphosphate carboxylase/oxygenase. Structure and origin of 2-carboxytetritol 1,4-bisphosphate, a novel O2-dependent side product generated by a site-directed mutant.
A signature of the oxygenase intermediate in catalysis by ribulose-bisphosphate carboxylase/oxygenase as provided by a site-directed mutant.
Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.
Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution.
The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.
In situ measurements of ribulose-1,5-bisphosphate carboxylase activity by nuclear magnetic resonance.
Multiple catalytic roles of His 287 of Rhodospirillum rubrum ribulose 1,5-bisphosphate carboxylase/oxygenase.
Mechanism of Rubisco: The Carbamate as General Base.
Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure.
Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry.
Complete spectra of the far-red chemiluminescence of the oxygenase reaction of Mn2+-activated ribulose-bisphosphate carboxylase/oxygenase establish excited Mn2+ as the source.
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized.
Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.
Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxygenase by concerted site-directed mutagenesis and chemical modification.
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.
Crystal structure of the active site of ribulose-bisphosphate carboxylase.
Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution.
Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution.
Functional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis.
Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
LYS 191;ASP 193;GLU 194(Magnesium binding)
LYS 189;ASP 191;GLU 192(Magnesium binding)
LYS 191; ;GLU 194(Magnesium binding)
LYS 186;ASP 188;GLU 189(Magnesium binding)