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Literature summary extracted from

  • 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.
    The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers (2014), Plant Cell, 26, 2996-3009.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
2.4.1.12 Oryza sativa Q84ZN6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.12 UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
 Oryza sativa UDP + [(1->4)-beta-D-glucosyl]n+1
-
 ?

Subunits

EC Number Subunits Comment 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

Synonyms

EC Number Synonyms Comment Organism
2.4.1.12 cellulose synthase
-
 Oryza sativa
2.4.1.12 CESA8
-
 Oryza sativa

General Information

EC Number General Information Comment 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