2.4.1.12: cellulose synthase (UDP-forming)
This is an abbreviated version!
For detailed information about cellulose synthase (UDP-forming), go to the full flat file.
Word Map on EC 2.4.1.12
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2.4.1.12
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cesas
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microfibrils
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synthases
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polysaccharide
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candida
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xylem
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echinocandins
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microtubule
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cotton
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lignin
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synthase-like
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hypocotyls
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chitin
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populus
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caspofungin
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acetobacter
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pectin
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hirsutum
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xyloglucan
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xylinum
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gossypium
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callose
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beta-glucans
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c-di-gmp
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wall-related
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candidiasis
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diguanylate
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1,3-beta-glucan
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micafungin
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load-bearing
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calcofluor
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expansin
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beta-1,3-glucan
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anidulafungin
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gluconacetobacter
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hemicelluloses
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rho1
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non-cellulosic
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aspen
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tremuloides
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analysis
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tracheary
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cslc
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hansenii
- 2.4.1.12
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cesas
- microfibrils
- synthases
- polysaccharide
- candida
- xylem
-
echinocandins
- microtubule
- cotton
- lignin
-
synthase-like
- hypocotyls
- chitin
- populus
- caspofungin
- acetobacter
- pectin
- hirsutum
- xyloglucan
- xylinum
- gossypium
- callose
- beta-glucans
- c-di-gmp
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wall-related
- candidiasis
- diguanylate
- 1,3-beta-glucan
- micafungin
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load-bearing
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calcofluor
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expansin
- beta-1,3-glucan
- anidulafungin
- gluconacetobacter
- hemicelluloses
- rho1
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non-cellulosic
- aspen
- tremuloides
- analysis
-
tracheary
- cslc
- hansenii
Reaction
Synonyms
1,4-beta-D-glucan synthase, 1,4-beta-glucan synthase, AcsA, AcsAB, AcsB, AtCesA7, BcsA-B, beta-1,4-glucan synthase, beta-1,4-glucan synthetase, beta-1,4-glucosyltransferase, beta-glucan synthase, cellulose syntethase, cellulose synthase, cellulose synthase (UDP-forming), cellulose synthase (uridine diphosphate-forming), cellulose synthase 2, cellulose synthase 3, cellulose synthase A, cellulose synthase A1, cellulose synthase A8, cellulose synthase complex, cellulose synthase-8, Ces A, CesA, CesA1, CesA2, CESA3, CESA4, CESA6, CESA7, CESA8, CSC, CSLD3, CslF, CslH, GhCesA1, glucan synthase, glucosyltransferase, uridine diphosphoglucose-1,4-beta-glucan, GS-I, GXY_04282, inner membrane-associated bacterial cellulose synthase, IRX3, More, UDP-glucose-1,4-beta-glucan glucosyltransferase, UDP-glucose-dependent beta-1,4-glucan synthase, UDP-glucose:1,4-beta-D-glucan 4-beta-D-glucosyltransferase, UDPglucose-beta-glucan glucosyltransferase, UDPglucose-cellulose glucosyltransferase, uridine diphosphoglucose-cellulose glucosyltransferase
ECTree
2.4.1.12 cellulose synthase (UDP-forming)Advanced search results
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General Information on EC 2.4.1.12 - cellulose synthase (UDP-forming)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
malfunction
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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
metabolism
physiological function
additional information
metabolism
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in the presence of required substrate (UDP-alpha-D-glucose) and all cofactors (cyclic diguanylate and Mg2+), the enzyme efficiently synthesizes cellulose microfibrils
metabolism
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the enzyme is not only sufficient for cellulose biosynthesis in vitro but also suffices to bundle individual glucan chains into cellulose microfibrils
physiological function
all CesA isozymes are directly involved in cellulose biosynthesis
physiological function
cellulose synthase is involved in the synthesis of the secondary cell wall
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
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CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
EgraCesA1 is involved in the cellulose biosynthesis machinery in wood formation
physiological function
EgraCesA2 is involved in the cellulose biosynthesis machinery in wood formation
physiological function
EgraCesA3 is involved in the cellulose biosynthesis machinery in wood formation
physiological function
the enzyme is involved in cellulose biosynthesis in secondary vascular tissue and biosynthesis of the secondary cell wall, rather than the primary, overview
physiological function
the SmCesA2 PH domain binds in vitro to phosphoinositides, F-actin and microtubules, and co-localizes with F-actin in vivo. The SmCesA2 PH domain has a role in the regulation, trafficking and/or targeting of the cell wall synthesizing enzyme
physiological 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
physiological function
in bacteria, cellulose synthesis and translocation is catalyzed by the inner membrane-associated bacterial cellulose synthase (Bcs)A and BcsB subunits. Similar to alginate and poly-beta-1,6 N-acetylglucosamine, bacterial cellulose is implicated in the formation of sessile bacterial communities, termed biofilms, and its synthesis is likewise stimulated by cyclic-di-GMP. The membrane-associated domain of BcsB is required for cellulose synthesis
physiological function
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the enzyme is implicated in secondary cell wall formation
additional information
BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
additional information
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BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
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
additional information
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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
additional information
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
additional information
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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
