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Results 1 - 10 of 18 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12evolution SmCesA2PH shares the PPBM motif with several PH domains of human proteins, the SmCesA2 PH domain is similar to the C-terminal PH domain of the human protein TAPP1 718750
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12malfunction the naturally occuring irx3-1 and irx5-2 mutations are caused by premature stop codons that result in protein truncation of CESA7 and CESA4,respectively. In the naturally occuring irx3-1 background, interaction between CESA4 and CESA8 is greatly reduced, and the proteins fail to localize to the plasma membrane 704608
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12metabolism in the presence of required substrate (UDP-alpha-D-glucose) and all cofactors (cyclic diguanylate and Mg2+), the enzyme efficiently synthesizes cellulose microfibrils 755703
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12metabolism the enzyme is not only sufficient for cellulose biosynthesis in vitro but also suffices to bundle individual glucan chains into cellulose microfibrils 758221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12more BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis 737161
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12more 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 736991
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12more structure of the BcsA-B translocation intermediate revealing the architecture of the cellulose synthase. Subunit BcsA forms a cellulose-conducting channel, modeling for the coupling of cellulose synthesis and translocation in which the nascent polysaccharide is extended by one glucose molecule at a time, overview 736877
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12physiological function all CesA isozymes are directly involved in cellulose biosynthesis 703825
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12physiological function cellulose synthase is involved in the synthesis of the secondary cell wall 703730
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.12physiological function cellulose synthases (CESAs) are membrane-embedded glycosyltransferases, which utilize UDP-activated glucose (UDP-Glc) to processively elongate the nascent polysaccharide in a reaction that inverts the configuration at the anomeric carbon of the newly added sugar from alpha to beta. Cellulose synthesis and transport across the inner bacterial membrane is mediated by a complex of the multi-spanning catalytic BcsA subunit and the membrane-anchored, periplasmic BcsB protein. Structure-function analysis and modeling, overview 736877
Results 1 - 10 of 18 > >>