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, 3-phospho-D-glycerate.
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, Mg(II), and activator CO2 at 2.3-A resolution.
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, ribulose-1,5-bisphosphate.
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, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase.
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. Structure and origin of 2-carboxytetritol 1,4-bisphosphate, a novel O2-dependent side product generated by a site-directed mutant.
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, Pyrococcus kodakaraensis KOD1.
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, all ribulose bisphosphate carboxylases may be nearly perfectly optimized.
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, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.
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, 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

Created Updated
2004-07-26 2010-04-22