DB code: D00542
CATH domain | 3.30.70.150 : Alpha-Beta Plaits | |
---|---|---|
3.20.20.110 : TIM Barrel | Catalytic domain | |
E.C. | 4.1.1.39 | |
CSA | 1rba | |
M-CSA | 1rba | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
O58677 |
Ribulose bisphosphate carboxylase
|
RuBisCO
EC 4.1.1.39 |
NP_142861.1
(Protein)
NC_000961.1 (DNA/RNA sequence) |
PF00016
(RuBisCO_large)
PF02788 (RuBisCO_large_N) [Graphical View] |
O93627 |
Ribulose bisphosphate carboxylase
|
RuBisCO
EC 4.1.1.39 |
YP_184703.1
(Protein)
NC_006624.1 (DNA/RNA sequence) |
PF00016
(RuBisCO_large)
PF02788 (RuBisCO_large_N) [Graphical View] |
P04718 |
Ribulose bisphosphate carboxylase
|
RuBisCO
EC 4.1.1.39 |
PF00016
(RuBisCO_large)
PF02788 (RuBisCO_large_N) [Graphical View] |
KEGG enzyme name |
---|
Ribulose-bisphosphate carboxylase
D-ribulose 1,5-diphosphate carboxylase D-ribulose-1,5-bisphosphate carboxylase RuBP carboxylase Carboxydismutase Diphosphoribulose carboxylase Ribulose 1,5-bisphosphate carboxylase Ribulose 1,5-bisphosphate carboxylase/oxygenase Ribulose 1,5-diphosphate carboxylase Ribulose 1,5-diphosphate carboxylase/oxygenase Ribulose bisphosphate carboxylase/oxygenase Ribulose diphosphate carboxylase Ribulose diphosphate carboxylase/oxygenase Rubisco |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
O58677 | RBL_PYRHO | 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2). | Homodimer (By similarity). | Binds 1 magnesium ion per subunit (By similarity). | |
O93627 | RBL_PYRKO | 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2). | Homodecamer, consisting of fiver dimer units which form a ring-like pentagonal structure. This arrangement is essential for its high thermostability. Composed solely of large subunits. | Binds 1 magnesium ion per subunit. | |
P04718 | RBL2_RHORU | 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2). | Homodimer. | Binds 1 magnesium ion per subunit. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00630 | Glyoxylate and dicarboxylate metabolism | |
MAP00710 | Carbon fixation |
Compound table | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||||||||
KEGG-id | C00305 | C01182 | C00011 | C00001 | C00007 | C00197 | C00988 | I00064 | I00065 | I00066 | |||||
E.C. |
(carboxylation & oxygenation)
|
(carboxylation)
|
(carboxylation)
|
(oxygenation)
|
(carboxylation & oxygenation)
|
(oxygenation)
|
(carboxynation & oxygenation)
|
(carboxylation)
|
(oxygenation)
|
||||||
Compound | Magnesium | D-Ribulose 1,5-bisphosphate | CO2 | H2O | O2 | 3-Phospho-D-glycerate | 2-Phosphoglycolate | 2,3-cis-enediol-D-ribulose-1,5-bisphosphate | 2-carboxy-3,3-diol-D-arabinitol-1,5-bisphosphate | 2-peroxy-3,3-diol-D-arabinitol-1,5-bisphosphate | |||||
Type | divalent metal (Ca2+, Mg2+) | carbohydrate,phosphate group/phosphate ion | others | H2O | others | carbohydrate,carboxyl group,phosphate group/phosphate ion | carboxyl group,phosphate group/phosphate ion | ||||||||
ChEBI |
18420 18420 |
16710 16710 |
16526 16526 |
15377 15377 |
15379 26689 27140 15379 26689 27140 |
17794 17794 |
17150 17150 |
||||||||
PubChem |
888 888 |
123658 123658 |
280 280 |
22247451 962 22247451 962 |
977 977 |
439183 439183 |
529 529 |
||||||||
2cwxA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cwxE01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeD01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69A01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69B01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69D01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69E01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehC01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehD01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehE01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rbaA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rbaB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rusA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rusB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rusA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rusB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5rubA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5rubB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
9rubA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
9rubB01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cwxA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cwxE02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeC02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2cxeD02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69A02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69B02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69D02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2d69E02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehC02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehD02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1gehE02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rbaA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rbaB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1rusA02 | Unbound | Unbound | Unbound | Unbound | Bound:3PG | Unbound | Unbound | Unbound | Unbound | ||||||
1rusB02 | Unbound | Unbound | Unbound | Unbound | Bound:3PG | Unbound | Unbound | Unbound | Unbound | ||||||
2rusA02 | Bound:_MG | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2rusB02 | Bound:_MG | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5rubA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5rubB02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
9rubA02 | Bound:_MG | Bound:RUB | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
9rubB02 | Bound:_MG | Bound:RUB | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [23] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
2cwxA01 | ||||||||||
2cwxE01 | ||||||||||
2cxeA01 | ||||||||||
2cxeB01 | ||||||||||
2cxeC01 | ||||||||||
2cxeD01 | ||||||||||
2d69A01 | ||||||||||
2d69B01 | ||||||||||
2d69D01 | ||||||||||
2d69E01 | ||||||||||
1gehA01 | ||||||||||
1gehB01 | ||||||||||
1gehC01 | ||||||||||
1gehD01 | ||||||||||
1gehE01 | ||||||||||
1rbaA01 | ||||||||||
1rbaB01 | ||||||||||
1rusA01 | ||||||||||
1rusB01 | ||||||||||
2rusA01 | ||||||||||
2rusB01 | ||||||||||
5rubA01 | ||||||||||
5rubB01 | ||||||||||
9rubA01 | ||||||||||
9rubB01 | ||||||||||
2cwxA02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2cwxE02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2cxeA02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2cxeB02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2cxeC02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2cxeD02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2d69A02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2d69B02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2d69D02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
2d69E02 | LYS 160;LYS 162;LYS 186;HIS 279;LYS 318 | LYS 186;ASP 188;GLU 189(Magnesium binding) | ASP 187 | |||||||
1gehA02 | LYS 163;LYS 165;LYS 189;HIS 281; | LYS 189;ASP 191;GLU 192(Magnesium binding) | ASP 190 | invisible 319-323 | ||||||
1gehB02 | LYS 163;LYS 165;LYS 189;HIS 281; | LYS 189;ASP 191;GLU 192(Magnesium binding) | ASP 190 | invisible 319-323 | ||||||
1gehC02 | LYS 163;LYS 165;LYS 189;HIS 281; | LYS 189;ASP 191;GLU 192(Magnesium binding) | ASP 190 | invisible 319-323 | ||||||
1gehD02 | LYS 163;LYS 165;LYS 189;HIS 281; | LYS 189;ASP 191;GLU 192(Magnesium binding) | ASP 190 | invisible 319-323 | ||||||
1gehE02 | LYS 163;LYS 165;LYS 189;HIS 281; | LYS 189;ASP 191;GLU 192(Magnesium binding) | ASP 190 | invisible 319-323 | ||||||
1rbaA02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;;GLU 194(Magnesium binding) | ASN 192 | mutant D193N, invisible 325-334 | ||||||
1rbaB02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;;GLU 194(Magnesium binding) | ASN 192 | mutant D193N, invisible 325-334 | ||||||
1rusA02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;ASP 193;GLU 194(Magnesium binding) | ASN 192 | invisible 326-333 | ||||||
1rusB02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;ASP 193;GLU 194(Magnesium binding) | ASN 192 | invisible 326-333 | ||||||
2rusA02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;ASP 193;GLU 194(Magnesium binding) | FOR 501 | ASN 192 | invisible 325-334, modified K191 | |||||
2rusB02 | LYS 166;LYS 168;LYS 191;HIS 287;LYS 329 | LYS 191;ASP 193;GLU 194(Magnesium binding) | FOR 501 | ASN 192 | invisible 326-331, modified K191 | |||||
5rubA02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;ASP 193;GLU 194(Magnesium binding) | ASN 192 | invisible 325-333 | ||||||
5rubB02 | LYS 166;LYS 168;LYS 191;HIS 287; | LYS 191;ASP 193;GLU 194(Magnesium binding) | ASN 192 | invisible 324-335 | ||||||
9rubA02 | LYS 166;LYS 168;LYS 191;HIS 287;LYS 329 | LYS 191;ASP 193;GLU 194(Magnesium binding) | FMT 601 | ASN 192 | modified K191 (carbamated) | |||||
9rubB02 | LYS 166;LYS 168;LYS 191;HIS 287;LYS 329 | LYS 191;ASP 193;GLU 194(Magnesium binding) | FMT 701 | ASN 192 | modified K191 (carbamated) |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[1]
|
Scheme I, p.484 | 3 |
[6]
|
Scheme I, p.990 | 5 |
[7]
|
FIGURE 1, p.905 | 3 |
[9]
|
FIG. 1, p.12605 | 5 |
[9]
|
FIG. 8A, p.12609 | 1 |
[10]
|
Figure 1, p.124 | 4 |
[13]
|
Figure 2, p.6 | 6 |
[13]
|
Figure 10, p.38 | 1 |
[15]
|
FIG. 8, p.25884 | 6 |
[16]
|
Figure 1, p.209 | 6 |
[17]
|
FIGURE 10, p.11304 | 2 |
[18]
|
FIG. 1, p.11742 | 5 |
[18]
|
FIG. 5, p.11743 | 3 |
[19]
|
Figure 1, p.161 | 5 |
[19]
|
Figure 2A, p.162 | 1 |
[19]
|
Figure 2B, p.162 | 1 |
[19]
|
Figure 8, p.168 | 5 |
[20]
|
Figue 1, p.439 | 7 |
[20]
|
Figue 7, p.440 | 8 |
[21]
|
SCHEME 1, p.27 | 3 |
[22]
|
Fig. 6, p.734 | 3 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3082286 |
Journal | Arch Biochem Biophys |
Year | 1986 |
Volume | 245 |
Pages | 483-93 |
Authors | Pierce J, Reddy GS |
Title | The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). |
Medline ID | |
PubMed ID | |
Journal | EMBO J |
Year | 1986 |
Volume | 5 |
Pages | 3409-15 |
Authors | Schneider G, Lindqvist Y, Braenden CI., Lorimer G |
Title | Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution. |
Related PDB | |
Related UniProtKB | P04718 |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2896501 |
Journal | Biochem Biophys Res Commun |
Year | 1988 |
Volume | 152 |
Pages | 579-84 |
Authors | Smith HB, Larimer FW, Hartman FC |
Title | Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxygenase by concerted site-directed mutagenesis and chemical modification. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 2492987 |
Journal | J Biol Chem |
Year | 1989 |
Volume | 264 |
Pages | 3643-6 |
Authors | Lundqvist T, Schneider G |
Title |
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, |
Related PDB | 1rus |
Related UniProtKB | |
[5] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
Medline ID | |
PubMed ID | |
Journal | Nature |
Year | 1989 |
Volume | 337 |
Pages | 229-34 |
Authors | Andersson I, Knight S, Schneider G, Lindqvist Y, Lundqvist T, Braenden CI, Lorimer GH |
Title | Crystal structure of the active site of ribulose-bisphosphate carboxylase. |
Related PDB | |
Related UniProtKB | P04718 |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
Medline ID | 90189156 |
PubMed ID | 2107319 |
Journal | J Mol Biol |
Year | 1990 |
Volume | 211 |
Pages | 989-1008 |
Authors | Schneider G, Lindqvist Y, Lundqvist T |
Title | Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution. |
Related PDB | 5rub |
Related UniProtKB | P04718 |
[7] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
Medline ID | 91113700 |
PubMed ID | 1899197 |
Journal | Biochemistry |
Year | 1991 |
Volume | 30 |
Pages | 904-8 |
Authors | Lundqvist T, Schneider G |
Title |
Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, |
Related PDB | 2rus |
Related UniProtKB | P04718 |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1761567 |
Journal | J Biol Chem |
Year | 1991 |
Volume | 266 |
Pages | 24734-40 |
Authors | Harpel MR, Larimer FW, Hartman FC |
Title | Functional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 1905726 |
Journal | J Biol Chem |
Year | 1991 |
Volume | 266 |
Pages | 12604-11 |
Authors | Lundqvist T, Schneider G |
Title |
Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, |
Related PDB | 9rub |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1525466 |
Journal | Annu Rev Biophys Biomol Struct |
Year | 1992 |
Volume | 21 |
Pages | 119-43 |
Authors | Schneider G, Lindqvist Y, Branden CI |
Title | RUBISCO: structure and mechanism. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 1606957 |
Journal | Eur J Biochem |
Year | 1992 |
Volume | 206 |
Pages | 729-35 |
Authors | Soderlind E, Schneider G, Gutteridge S |
Title | Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes. |
Related PDB | 1rba |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1569095 |
Journal | J Biol Chem |
Year | 1992 |
Volume | 267 |
Pages | 8452-7 |
Authors | Soper TS, Larimer FW, Mural RJ, Lee EH, Hartman FC |
Title | Role of asparagine-111 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as explored by site-directed mutagenesis. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8322615 |
Journal | Adv Enzymol Relat Areas Mol Biol |
Year | 1993 |
Volume | 67 |
Pages | 1-75 |
Authors | Hartman FC, Harpel MR |
Title | Chemical and genetic probes of the active site of D-ribulose-1,5-bisphosphate carboxylase/oxygenase: a retrospective based on the three-dimensional structure. |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8253788 |
Journal | J Biol Chem |
Year | 1993 |
Volume | 268 |
Pages | 26583-91 |
Authors | Lee EH, Harpel MR, Chen YR, Hartman FC |
Title | Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase. |
Related PDB | |
Related UniProtKB | |
[15] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). |
Medline ID | 94064666 |
PubMed ID | 8245022 |
Journal | J Biol Chem |
Year | 1993 |
Volume | 268 |
Pages | 25876-86 |
Authors | Newman J, Gutteridge S |
Title | The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution. |
Related PDB | |
Related UniProtKB | P00880 P04716 |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7979237 |
Journal | Annu Rev Biochem |
Year | 1994 |
Volume | 63 |
Pages | 197-234 |
Authors | Hartman FC, Harpel MR |
Title |
Structure, |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7669788 |
Journal | Biochemistry |
Year | 1995 |
Volume | 34 |
Pages | 11296-306 |
Authors | Harpel MR, Serpersu EH, Lamerdin JA, Huang ZH, Gage DA, Hartman FC |
Title |
Oxygenation mechanism of ribulose-bisphosphate carboxylase/oxygenase. |
Related PDB | |
Related UniProtKB | |
[18] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7744819 |
Journal | J Biol Chem |
Year | 1995 |
Volume | 270 |
Pages | 11741-4 |
Authors | Chen YR, Hartman FC |
Title | A signature of the oxygenase intermediate in catalysis by ribulose-bisphosphate carboxylase/oxygenase as provided by a site-directed mutant. |
Related PDB | |
Related UniProtKB | |
[19] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). |
Medline ID | 96240687 |
PubMed ID | 8648644 |
Journal | J Mol Biol |
Year | 1996 |
Volume | 259 |
Pages | 160-74 |
Authors | Andersson I |
Title | Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate. |
Related PDB | 8rub 8ruc |
Related UniProtKB | P00875 P00870 |
[20] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). |
Medline ID | 97186746 |
PubMed ID | 9034362 |
Journal | J Mol Biol |
Year | 1997 |
Volume | 265 |
Pages | 432-44 |
Authors | Taylor TC, Andersson I |
Title | The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate. |
Related PDB | 1rxo 1rcx |
Related UniProtKB | P00875 P00870 |
[21] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9512768 |
Journal | Anal Biochem |
Year | 1998 |
Volume | 257 |
Pages | 26-32 |
Authors | Wang ZY, Luo S, Sato K, Kobayashi M, Nozawa T |
Title | In situ measurements of ribulose-1,5-bisphosphate carboxylase activity by nuclear magnetic resonance. |
Related PDB | |
Related UniProtKB | |
[22] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9541405 |
Journal | Protein Sci |
Year | 1998 |
Volume | 7 |
Pages | 730-8 |
Authors | Harpel MR, Larimer FW, Hartman FC |
Title | Multiple catalytic roles of His 287 of Rhodospirillum rubrum ribulose 1,5-bisphosphate carboxylase/oxygenase. |
Related PDB | |
Related UniProtKB | |
[23] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11848907 |
Journal | Chem Rev |
Year | 1998 |
Volume | 98 |
Pages | 549-562 |
Authors | Cleland WW, Andrews TJ, Gutteridge S, Hartman FC, Lorimer GH |
Title | Mechanism of Rubisco: The Carbamate as General Base. |
Related PDB | |
Related UniProtKB | |
[24] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9988755 |
Journal | J Biol Chem |
Year | 1999 |
Volume | 274 |
Pages | 5078-82 |
Authors | Ezaki S, Maeda N, Kishimoto T, Atomi H, Imanaka T |
Title |
Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, |
Related PDB | |
Related UniProtKB | |
[25] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10512715 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 293 |
Pages | 57-66 |
Authors | Maeda N, Kitano K, Fukui T, Ezaki S, Atomi H, Miki K, Imanaka T |
Title | Ribulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure. |
Related PDB | |
Related UniProtKB | |
[26] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11435112 |
Journal | Structure (Camb) |
Year | 2001 |
Volume | 9 |
Pages | 473-81 |
Authors | Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K |
Title | Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry. |
Related PDB | 1geh |
Related UniProtKB | |
[27] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12604603 |
Journal | J Biol Chem |
Year | 2003 |
Volume | 278 |
Pages | 16488-93 |
Authors | Lilley RM, Wang X, Krausz E, Andrews TJ |
Title | Complete spectra of the far-red chemiluminescence of the oxygenase reaction of Mn2+-activated ribulose-bisphosphate carboxylase/oxygenase establish excited Mn2+ as the source. |
Related PDB | |
Related UniProtKB | |
[28] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 16641091 |
Journal | Proc Natl Acad Sci U S A |
Year | 2006 |
Volume | 103 |
Pages | 7246-51 |
Authors | Tcherkez GG, Farquhar GD, Andrews TJ |
Title |
Despite slow catalysis and confused substrate specificity, |
Related PDB | |
Related UniProtKB | |
[29] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18281717 |
Journal | J Exp Bot |
Year | 2008 |
Volume | 59 |
Pages | 1515-24 |
Authors | Tabita FR, Satagopan S, Hanson TE, Kreel NE, Scott SS |
Title |
Distinct form I, |
Related PDB | |
Related UniProtKB | |
[30] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18294858 |
Journal | Plant Physiol Biochem |
Year | 2008 |
Volume | 46 |
Pages | 275-91 |
Authors | Andersson I, Backlund A |
Title | Structure and function of Rubisco. |
Related PDB | |
Related UniProtKB | |
[31] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18417482 |
Journal | J Exp Bot |
Year | 2008 |
Volume | 59 |
Pages | 1555-68 |
Authors | Andersson I |
Title | Catalysis and regulation in Rubisco. |
Related PDB | |
Related UniProtKB |
Comments |
---|
For the enzyme, Currently, This enzyme catalyzes the incorporation of atmospheric CO2 into the organic molecule, 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 |
Created | Updated |
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2004-07-26 | 2010-04-22 |