EzCatDB: D00542
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DB codeD00542
CATH domainDomain 13.30.70.150 : Alpha-Beta Plaits
Domain 23.20.20.110 : TIM BarrelCatalytic domain
E.C.4.1.1.39
CSA1rba


Enzyme Name
UniProtKBKEGG

O58677O93627P04718
Protein nameRibulose bisphosphate carboxylaseRibulose bisphosphate carboxylaseRibulose bisphosphate carboxylaseRibulose-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
SynonymsRuBisCO
EC 4.1.1.39
RuBisCO
EC 4.1.1.39
RuBisCO
EC 4.1.1.39
RefSeqNP_142861.1 (Protein)
NC_000961.1 (DNA/RNA sequence)
YP_184703.1 (Protein)
NC_006624.1 (DNA/RNA sequence)

PfamPF00016 (RuBisCO_large)
PF02788 (RuBisCO_large_N)
[Graphical view]
PF00016 (RuBisCO_large)
PF02788 (RuBisCO_large_N)
[Graphical view]
PF00016 (RuBisCO_large)
PF02788 (RuBisCO_large_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00630Glyoxylate and dicarboxylate metabolism
MAP00710Carbon fixation

UniProtKB:Accession NumberO58677O93627P04718
Entry nameRBL_PYRHORBL_PYRKORBL2_RHORU
Activity2 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).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).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).
SubunitHomodimer (By similarity).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.Homodimer.
Subcellular location


CofactorBinds 1 magnesium ion per subunit (By similarity).Binds 1 magnesium ion per subunit.Binds 1 magnesium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00305C01182C00011C00001C00007C00197C00988I00064I00065I00066
E.C.
(carboxylation & oxygenation)(carboxylation)(carboxylation)(oxygenation)(carboxylation & oxygenation)(oxygenation)(carboxynation & oxygenation)(carboxylation)(oxygenation)
CompoundMagnesiumD-Ribulose 1,5-bisphosphateCO2H2OO23-Phospho-D-glycerate2-Phosphoglycolate2,3-cis-enediol-D-ribulose-1,5-bisphosphate2-carboxy-3,3-diol-D-arabinitol-1,5-bisphosphate2-peroxy-3,3-diol-D-arabinitol-1,5-bisphosphate
Typedivalent metal (Ca2+, Mg2+)carbohydrate,phosphate group/phosphate ionothersH2Ootherscarbohydrate,carboxyl group,phosphate group/phosphate ioncarboxyl group,phosphate group/phosphate ion


ChEBI18420
16710
16526
15377
27140
26689
15379
17794
17150



PubChem888
123658
280
962
22247451
977
439183
529



                  
2cwxA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cwxE01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeC01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeD01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69A01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69B01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69D01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69E01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehC01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehD01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehE01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rbaA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rbaB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rusA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rusB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2rusA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2rusB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
5rubA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
5rubB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
9rubA01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
9rubB01UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cwxA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cwxE02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeB02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeC02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2cxeD02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69A02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69B02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69D02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2d69E02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehB02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehC02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehD02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1gehE02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rbaA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rbaB02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
1rusA02UnboundUnboundUnbound UnboundBound:3PGUnboundUnboundUnboundUnbound
1rusB02UnboundUnboundUnbound UnboundBound:3PGUnboundUnboundUnboundUnbound
2rusA02Bound:_MGUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
2rusB02Bound:_MGUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
5rubA02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
5rubB02UnboundUnboundUnbound UnboundUnboundUnboundUnboundUnboundUnbound
9rubA02Bound:_MGBound:RUBUnbound UnboundUnboundUnboundUnboundUnboundUnbound
9rubB02Bound:_MGBound:RUBUnbound UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [23]
pdbCatalytic residuesCofactor-binding residuesModified residuesMain-chain involved in catalysiscomment
             
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 
 
 
 
 
2cwxA02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2cwxE02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2cxeA02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2cxeB02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2cxeC02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2cxeD02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2d69A02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2d69B02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2d69D02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
2d69E02LYS 160;LYS 162;LYS 186;HIS 279;LYS 318
LYS 186;ASP 188;GLU 189(Magnesium binding)
       
ASP 187
 
1gehA02LYS 163;LYS 165;LYS 189;HIS 281;       
LYS 189;ASP 191;GLU 192(Magnesium binding)
       
ASP 190
invisible 319-323
1gehB02LYS 163;LYS 165;LYS 189;HIS 281;       
LYS 189;ASP 191;GLU 192(Magnesium binding)
       
ASP 190
invisible 319-323
1gehC02LYS 163;LYS 165;LYS 189;HIS 281;       
LYS 189;ASP 191;GLU 192(Magnesium binding)
       
ASP 190
invisible 319-323
1gehD02LYS 163;LYS 165;LYS 189;HIS 281;       
LYS 189;ASP 191;GLU 192(Magnesium binding)
       
ASP 190
invisible 319-323
1gehE02LYS 163;LYS 165;LYS 189;HIS 281;       
LYS 189;ASP 191;GLU 192(Magnesium binding)
       
ASP 190
invisible 319-323
1rbaA02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;       ;GLU 194(Magnesium binding)
       
ASN 192
mutant D193N, invisible 325-334
1rbaB02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;       ;GLU 194(Magnesium binding)
       
ASN 192
mutant D193N, invisible 325-334
1rusA02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;ASP 193;GLU 194(Magnesium binding)
       
ASN 192
invisible 326-333
1rusB02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;ASP 193;GLU 194(Magnesium binding)
       
ASN 192
invisible 326-333
2rusA02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;ASP 193;GLU 194(Magnesium binding)
FOR 501
ASN 192
invisible 325-334, modified K191
2rusB02LYS 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
5rubA02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;ASP 193;GLU 194(Magnesium binding)
       
ASN 192
invisible 325-333
5rubB02LYS 166;LYS 168;LYS 191;HIS 287;       
LYS 191;ASP 193;GLU 194(Magnesium binding)
       
ASN 192
invisible 324-335
9rubA02LYS 166;LYS 168;LYS 191;HIS 287;LYS 329
LYS 191;ASP 193;GLU 194(Magnesium binding)
FMT 601
ASN 192
modified K191 (carbamated)
9rubB02LYS 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
ReferencesSectionsNo. of steps in catalysis
[1]Scheme I, p.4843
[6]Scheme I, p.9905
[7]FIGURE 1, p.9053
[9]FIG. 1, p.126055
[9]FIG. 8A, p.126091
[10]Figure 1, p.1244
[13]Figure 2, p.66
[13]Figure 10, p.381
[15]FIG. 8, p.258846
[16]Figure 1, p.2096
[17]FIGURE 10, p.113042
[18]FIG. 1, p.117425
[18]FIG. 5, p.117433
[19]Figure 1, p.1615
[19]Figure 2A, p.1621
[19]Figure 2B, p.1621
[19]Figure 8, p.1685
[20]Figue 1, p.4397
[20]Figue 7, p.4408
[21]SCHEME 1, p.273
[22]Fig. 6, p.7343

references
[1]
PubMed ID3082286
JournalArch Biochem Biophys
Year1986
Volume245
Pages483-93
AuthorsPierce J, Reddy GS
TitleThe sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
JournalEMBO J
Year1986
Volume5
Pages3409-15
AuthorsSchneider G, Lindqvist Y, Braenden CI., Lorimer G
TitleThree-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution.
Related UniProtKBP04718
[3]
PubMed ID2896501
JournalBiochem Biophys Res Commun
Year1988
Volume152
Pages579-84
AuthorsSmith HB, Larimer FW, Hartman FC
TitleSubtle alteration of the active site of ribulose bisphosphate carboxylase/oxygenase by concerted site-directed mutagenesis and chemical modification.
[4]
CommentsX-ray crystallography
PubMed ID2492987
JournalJ Biol Chem
Year1989
Volume264
Pages3643-6
AuthorsLundqvist T, Schneider G
TitleCrystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate.
Related PDB1rus
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
JournalNature
Year1989
Volume337
Pages229-34
AuthorsAndersson I, Knight S, Schneider G, Lindqvist Y, Lundqvist T, Braenden CI, Lorimer GH
TitleCrystal structure of the active site of ribulose-bisphosphate carboxylase.
Related UniProtKBP04718
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID90189156
PubMed ID2107319
JournalJ Mol Biol
Year1990
Volume211
Pages989-1008
AuthorsSchneider G, Lindqvist Y, Lundqvist T
TitleCrystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution.
Related PDB5rub
Related UniProtKBP04718
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID91113700
PubMed ID1899197
JournalBiochemistry
Year1991
Volume30
Pages904-8
AuthorsLundqvist T, Schneider G
TitleCrystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution.
Related PDB2rus
Related UniProtKBP04718
[8]
PubMed ID1761567
JournalJ Biol Chem
Year1991
Volume266
Pages24734-40
AuthorsHarpel MR, Larimer FW, Hartman FC
TitleFunctional analysis of the putative catalytic bases His-321 and Ser-368 of Rhodospirillum rubrum ribulose bisphosphate carboxylase/oxygenase by site-directed mutagenesis.
[9]
CommentsX-ray crystallography
PubMed ID1905726
JournalJ Biol Chem
Year1991
Volume266
Pages12604-11
AuthorsLundqvist T, Schneider G
TitleCrystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
Related PDB9rub
[10]
PubMed ID1525466
JournalAnnu Rev Biophys Biomol Struct
Year1992
Volume21
Pages119-43
AuthorsSchneider G, Lindqvist Y, Branden CI
TitleRUBISCO: structure and mechanism.
[11]
CommentsX-ray crystallography
PubMed ID1606957
JournalEur J Biochem
Year1992
Volume206
Pages729-35
AuthorsSoderlind E, Schneider G, Gutteridge S
TitleSubstitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes.
Related PDB1rba
[12]
PubMed ID1569095
JournalJ Biol Chem
Year1992
Volume267
Pages8452-7
AuthorsSoper TS, Larimer FW, Mural RJ, Lee EH, Hartman FC
TitleRole of asparagine-111 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as explored by site-directed mutagenesis.
[13]
PubMed ID8322615
JournalAdv Enzymol Relat Areas Mol Biol
Year1993
Volume67
Pages1-75
AuthorsHartman FC, Harpel MR
TitleChemical and genetic probes of the active site of D-ribulose-1,5-bisphosphate carboxylase/oxygenase: a retrospective based on the three-dimensional structure.
[14]
PubMed ID8253788
JournalJ Biol Chem
Year1993
Volume268
Pages26583-91
AuthorsLee EH, Harpel MR, Chen YR, Hartman FC
TitlePerturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID94064666
PubMed ID8245022
JournalJ Biol Chem
Year1993
Volume268
Pages25876-86
AuthorsNewman J, Gutteridge S
TitleThe X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution.
Related UniProtKBP00880,P04716
[16]
PubMed ID7979237
JournalAnnu Rev Biochem
Year1994
Volume63
Pages197-234
AuthorsHartman FC, Harpel MR
TitleStructure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase.
[17]
PubMed ID7669788
JournalBiochemistry
Year1995
Volume34
Pages11296-306
AuthorsHarpel MR, Serpersu EH, Lamerdin JA, Huang ZH, Gage DA, Hartman FC
TitleOxygenation 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.
[18]
PubMed ID7744819
JournalJ Biol Chem
Year1995
Volume270
Pages11741-4
AuthorsChen YR, Hartman FC
TitleA signature of the oxygenase intermediate in catalysis by ribulose-bisphosphate carboxylase/oxygenase as provided by a site-directed mutant.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Medline ID96240687
PubMed ID8648644
JournalJ Mol Biol
Year1996
Volume259
Pages160-74
AuthorsAndersson I
TitleLarge structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.
Related PDB8rub,8ruc
Related UniProtKBP00875,P00870
[20]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID97186746
PubMed ID9034362
JournalJ Mol Biol
Year1997
Volume265
Pages432-44
AuthorsTaylor TC, Andersson I
TitleThe structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate.
Related PDB1rxo,1rcx
Related UniProtKBP00875,P00870
[21]
PubMed ID9512768
JournalAnal Biochem
Year1998
Volume257
Pages26-32
AuthorsWang ZY, Luo S, Sato K, Kobayashi M, Nozawa T
TitleIn situ measurements of ribulose-1,5-bisphosphate carboxylase activity by nuclear magnetic resonance.
[22]
PubMed ID9541405
JournalProtein Sci
Year1998
Volume7
Pages730-8
AuthorsHarpel MR, Larimer FW, Hartman FC
TitleMultiple catalytic roles of His 287 of Rhodospirillum rubrum ribulose 1,5-bisphosphate carboxylase/oxygenase.
[23]
PubMed ID11848907
JournalChem Rev
Year1998
Volume98
Pages549-562
AuthorsCleland WW, Andrews TJ, Gutteridge S, Hartman FC, Lorimer GH
TitleMechanism of Rubisco: The Carbamate as General Base.
[24]
PubMed ID9988755
JournalJ Biol Chem
Year1999
Volume274
Pages5078-82
AuthorsEzaki S, Maeda N, Kishimoto T, Atomi H, Imanaka T
TitlePresence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.
[25]
PubMed ID10512715
JournalJ Mol Biol
Year1999
Volume293
Pages57-66
AuthorsMaeda N, Kitano K, Fukui T, Ezaki S, Atomi H, Miki K, Imanaka T
TitleRibulose bisphosphate carboxylase/oxygenase from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 is composed solely of large subunits and forms a pentagonal structure.
[26]
PubMed ID11435112
JournalStructure (Camb)
Year2001
Volume9
Pages473-81
AuthorsKitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K
TitleCrystal structure of a novel-type archaeal rubisco with pentagonal symmetry.
Related PDB1geh
[27]
PubMed ID12604603
JournalJ Biol Chem
Year2003
Volume278
Pages16488-93
AuthorsLilley RM, Wang X, Krausz E, Andrews TJ
TitleComplete spectra of the far-red chemiluminescence of the oxygenase reaction of Mn2+-activated ribulose-bisphosphate carboxylase/oxygenase establish excited Mn2+ as the source.
[28]
PubMed ID16641091
JournalProc Natl Acad Sci U S A
Year2006
Volume103
Pages7246-51
AuthorsTcherkez GG, Farquhar GD, Andrews TJ
TitleDespite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized.
[29]
PubMed ID18281717
JournalJ Exp Bot
Year2008
Volume59
Pages1515-24
AuthorsTabita FR, Satagopan S, Hanson TE, Kreel NE, Scott SS
TitleDistinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.
[30]
PubMed ID18294858
JournalPlant Physiol Biochem
Year2008
Volume46
Pages275-91
AuthorsAndersson I, Backlund A
TitleStructure and function of Rubisco.
[31]
PubMed ID18417482
JournalJ Exp Bot
Year2008
Volume59
Pages1555-68
AuthorsAndersson I
TitleCatalysis and regulation in Rubisco.

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

createdupdated
2004-07-262010-04-22


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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