BRENDA - Enzyme Database show

The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers

Olek, A.T.; Rayon, C.; Makowski, L.; Kim, H.R.; Ciesielski, P.; Badger, J.; Paul, L.N.; Ghosh, S.; Kihara, D.; Crowley, M.; Himmel, M.E.; Bolin, J.T.; Carpita, N.C.; Plant Cell 26, 2996-3009 (2014)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
2.4.1.12
solution X-ray scattering of monomeric and dimeric catalytic subunits with or without bound substrate UDP-glucose
Oryza sativa
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Oryza sativa
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.12
Oryza sativa
Q84ZN6
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736991
Oryza sativa
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.12
dimer
recombinant catalytic domains of rice CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. The monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain, structure comparison and modeling, overview. Proposed role for dimers in particle rosette assembly
Oryza sativa
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.4.1.12
solution X-ray scattering of monomeric and dimeric catalytic subunits with or without bound substrate UDP-glucose
Oryza sativa
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Oryza sativa
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
736991
Oryza sativa
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.12
dimer
recombinant catalytic domains of rice CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. The monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain, structure comparison and modeling, overview. Proposed role for dimers in particle rosette assembly
Oryza sativa
General Information
EC Number
General Information
Commentary
Organism
2.4.1.12
additional information
binding kinetics indicate that each monomer of the dimeric enzyme independently synthesizes single glucan chains of cellulose, i.e. two chains per dimer pair. Strong conservation of the four catalytic motifs essential for binding to a UDP moiety, the diphosphate of UDP-Glc, and the nonreducing terminal cellobiosyl unit of the beta-D-glucan chain that extends into the protein, structure comparison and modeling, overview. The monomer and dimer of catalytic domain CatD bind specifically UDP and UDP-glucose
Oryza sativa
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.4.1.12
additional information
binding kinetics indicate that each monomer of the dimeric enzyme independently synthesizes single glucan chains of cellulose, i.e. two chains per dimer pair. Strong conservation of the four catalytic motifs essential for binding to a UDP moiety, the diphosphate of UDP-Glc, and the nonreducing terminal cellobiosyl unit of the beta-D-glucan chain that extends into the protein, structure comparison and modeling, overview. The monomer and dimer of catalytic domain CatD bind specifically UDP and UDP-glucose
Oryza sativa