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
Ribulose 1,5-bisphosphate carboxylase/oxygenase
Ribulose 1,5-diphosphate carboxylase/oxygenase
Ribulose bisphosphate carboxylase/oxygenase
Ribulose diphosphate carboxylase/oxygenase
LYS 186;ASP 188;GLU 189(Magnesium binding)
LYS 189;ASP 191;GLU 192(Magnesium binding)
LYS 191; ;GLU 194(Magnesium binding)
LYS 191;ASP 193;GLU 194(Magnesium binding)
Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
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.
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.
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.
The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain.
Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution.
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.
Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.