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Enzyme Nomenclature
Information on EC 2.4.1.12 - cellulose synthase (UDP-forming)
Word Map on EC 2.4.1.12
- 2.4.1.12
- candida
-
cesas
-
antifungal
-
echinocandins
- albicans
- caspofungin
-
microfibrils
- chitin
- xylem
- 1,3-beta-glucan
-
lipopeptide
- callose
- candidiasis
- xyloglucan
- beta-1,3-glucan
-
micafungin
-
anidulafungin
- cilofungin
- papulacandins
- pneumocandins
- udp-glc
-
synthase-like
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.4.1.12
-
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RECOMMENDED NAME
GeneOntology No.
cellulose synthase (UDP-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + [(1->4)-beta-D-glucosyl]n = UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(1->4)-beta-D-glucan 4-beta-D-glucosyltransferase
Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
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CAS REGISTRY NUMBER
COMMENTARY
9027-19-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a hybrid of Populus alba x Populus tremula, several cesA genes
-
-
spp. parvifolia, collected in Semengoh Forest Reservat, Kuching, Sarawak, Malaysia, gene SpcesA1
UniProt
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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
-
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
physiological function
additional information
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
cellulose synthase is involved in the synthesis of the secondary cell wall; cellulose synthase is involved in the synthesis of the secondary cell wall; cellulose synthase is involved in the synthesis of the secondary cell wall
physiological function
all CesA isozymes are directly involved in cellulose biosynthesis; all CesA isozymes are directly involved in cellulose biosynthesis
physiological function
EgraCesA1 is involved in the cellulose biosynthesis machinery in wood formation; EgraCesA1 is involved in the cellulose biosynthesis machinery in wood formation; EgraCesA2 is involved in the cellulose biosynthesis machinery in wood formation; EgraCesA2 is involved in the cellulose biosynthesis machinery in wood formation; EgraCesA3 is involved in the cellulose biosynthesis machinery in wood formation
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
physiological function
-
CesA is a central catalyst in the generation of the plant cell wall biomass
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
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
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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BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
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-
-
?
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
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-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
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?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
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-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
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-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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involved in the synthesis of cellulose
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UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
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?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
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-
-
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-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
?
additional information
?
-
-
cellulose synthase activity influences microtubule cortical array organization
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-
-
additional information
?
-
phosphorylation and subsequent degradation via a proteasome dependant pathway is a possible mechanism by which plants regulate the relative levels of the different cellulose synthase catalytic subunits that are essential for cellulose synthesis
-
-
-
additional information
?
-
procuste1 (prc1-1) cellulose deficient mutant of Arabidopsis is mutated in the cellulose synthase CESA6 gene resulting in a reduction in the cellulose content of the cell walls. RHD6 acts upstream of the normal cell wall loosening event which involves EXP7 expression. In the absence of a functional RHD6 the loosening and accompanying EXP7 expression is blocked. In the prc1-1 mutant background, the requirement for RHD6 during hair initiation is reduced which may result from a weaker cell wall structure mimicking the cell wall loosening events during hair formation
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-
additional information
?
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cellulose synthase A is a catalytic component of the cellulose synthase complex
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additional information
?
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interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
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-
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additional information
?
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interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
-
-
-
additional information
?
-
interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
-
-
-
additional information
?
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several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
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additional information
?
-
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
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-
additional information
?
-
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
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-
additional information
?
-
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
-
several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
-
-
-
additional information
?
-
-
several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
-
-
-
additional information
?
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Cellulose synthesis in Phytophthora infestans is required for normal appressorium formation and successful infection of potato
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additional information
?
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UDP-glucose acts as glycosyl donor in glucan synthesis, product analysis
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-
additional information
?
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UDP-glucose acts as glycosyl donor in glucan synthesis, product analysis
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-
additional information
?
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UDP-glucose acts as glycosyl donor in glucan synthesis, product analysis
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-
additional information
?
-
CesA2 binds in vitro to phosphoinositides, F-actin and microtubules via its PH domain, and co-localizes with F-actin in vivo
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
Q84ZN6
-
-
-
?
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
Q3J125
-
-
-
?
UDP-glucose + [(1->4)-beta-D-glucosyl]n
UDP + [(1->4)-beta-D-glucosyl]n+1
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-
-
-
?
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
P19449
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
involved in the synthesis of cellulose
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
UDPglucose + (1,4-beta-D-glucosyl)n
UDP + (1,4-beta-D-glucosyl)n+1
-
-
-
-
-
additional information
?
-
-
cellulose synthase activity influences microtubule cortical array organization
-
-
-
additional information
?
-
Q9SWW6
phosphorylation and subsequent degradation via a proteasome dependant pathway is a possible mechanism by which plants regulate the relative levels of the different cellulose synthase catalytic subunits that are essential for cellulose synthesis
-
-
-
additional information
?
-
Q94JQ6
procuste1 (prc1-1) cellulose deficient mutant of Arabidopsis is mutated in the cellulose synthase CESA6 gene resulting in a reduction in the cellulose content of the cell walls. RHD6 acts upstream of the normal cell wall loosening event which involves EXP7 expression. In the absence of a functional RHD6 the loosening and accompanying EXP7 expression is blocked. In the prc1-1 mutant background, the requirement for RHD6 during hair initiation is reduced which may result from a weaker cell wall structure mimicking the cell wall loosening events during hair formation
-
-
-
additional information
?
-
-
cellulose synthase A is a catalytic component of the cellulose synthase complex
-
-
-
additional information
?
-
Q84JA6
interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
-
-
-
additional information
?
-
Q8LPK5
interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
-
-
-
additional information
?
-
Q9SWW6
interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall, overview
-
-
-
additional information
?
-
-
several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
-
-
-
additional information
?
-
B1NYI6
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
B1NYI7
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
B1NYI9
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
B1NYJ0
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
Q2IB43
presence of at least two types of cellulose biosynthesis machinery in wood formation
-
-
-
additional information
?
-
-
several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
-
-
-
additional information
?
-
-
several genes from the cellulose synthase-like, Csl, family are involved in the synthesis of various hemicellulosic glycans. Mechanism of beta-glycan chain elongation, overview
-
-
-
additional information
?
-
-
Cellulose synthesis in Phytophthora infestans is required for normal appressorium formation and successful infection of potato
-
-
-
additional information
?
-
C9WPJ9
CesA2 binds in vitro to phosphoinositides, F-actin and microtubules via its PH domain, and co-localizes with F-actin in vivo
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Zn2+
the cotton fiber zinc-binding domain of cellulose synthase A1 displays rapid turnover in vitro and in vivo
Ca2+
-
divalent cation required, Ca2+ and Mg2+, 0.5-1.0 mM are effective for full activation
Mg2+
-
divalent cation required, Ca2+ and Mg2+, 0.5-1.0 mM are effective for full activation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorobenzonitrile
affects mycelial growth; affects mycelial growth
isoxaben
-
reduces cellulose synthesis in wild-type but not ixr1-1 seedlings
nucleoside phosphates
-
degree of inhibition in decreasing order: nucleoside-triphosphate, nucleoside-diphosphate, nucleoside-monophosphate
additional information
-
no inhibition by guanosine and adenosine diphosphates
-
UDP
-
BcsA-B undergoes feedback inhibition by UDP, competitive versus UDP-glucose. This inhibitory effect becomes rate limiting as the concentration of UDP-alpha-D-glucose exceeds that of UDP by about an order of magnitude
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cellodextrins
-
stimulate cellulose synthesis, cellulose synthesis is dependent on presence of a soluble primer
-
cyclic-3',5'-diguanylate
-
activates cellulose synthesis allosterically and binds BcsA-B with high affinity. The tight association of BcsA's PilZ and GT domains suggests that cyclic-3',5'-diguanylate controls the accessibility of the GT active site. Titrating UDP-Glc at different cyclic-3',5'-diguanylate concentrations shows that the maximum catalytic activity achieved depends on the overall c-di-GMP concentration, whereas the apparent affinity for UDP-Glc remains within 0.1-1.0 mM, comparable with the Km of 0.5 mM for UDP-Glc determined in the presence of 0.030 mM cyclic-3',5'-diguanylate. The cyclic-3',5'-diguanylate binding PilZ domain of cellulose synthase is a part of the catalytic BcsA subunit. Cyclic-3',5'-diguanylate does not alter BcsA's apparent affinity for UDP-Glc, yet it increases BcsA's apparent catalytic rate in vitro at least 10fold
cyclic-di-GMP
-
BcsA contains a PilZ domain within its C-terminal, intracellular domain and its activity is strongly stimulated by the bacterial secondary messenger cyclic-di-GMP
Polyethylene glycol
-
activation by polyethylene glycol and GTP is cooperative and involves association of the enzyme with a protein factor essential for high rates of enzyme activity
GTP
-
activation by polyethylene glycol and GTP is cooperative and involves association of the enzyme with a protein factor essential for high rates of enzyme activity
additional information
-
of membrane-bound enzyme; regulatory properties
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
monophasic Michaelis-Menten kinetics, kinetic analysis of cellulose synthesis, overview
-
1 - 2.5
UDPglucose
-
pH 7.5, 35°C, depending on individual membrane preparation
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.3
-
pH 6.5: 13% of activity maximum, pH 7.5: 39% of activity maximum, pH 8.3: activity maximum, enzyme is not tested under more alkaline conditions because of instability of UDPglucose
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
comparisons of morphologies of wild-type and mutant plant embryos and seedlings, overview
-
m-RNA expression high in developing seedlings and low in later growth stages
CESA3 and CESA6 are undetectable in imbibed seeds and appear after germination; CESA3 and CESA6 are undetectable in imbibed seeds and appear after germination
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m-RNA expression high in elongating stems and low in stems where secondary wall synthesis takes place
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long, cylindrical cells, movement of the cellulose synthase complexes beneath the nascent secondary wall in developing xylem vessels, quantitative analysis, overview
of eucalyptus undergoing secondary cell wall biosynthesis; of eucalyptus undergoing secondary cell wall biosynthesis; of eucalyptus undergoing secondary cell wall biosynthesis; of eucalyptus undergoing secondary cell wall biosynthesis; of eucalyptus undergoing secondary cell wall biosynthesis
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
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cortical, the cellulose synthase-containing compartment moves rapidly beneath sites of secondary wall synthesis, overview
additional information
CesA2 might co-localize with microtubules in vivo
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secondary; secondary; secondary; secondary; secondary
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cellulose synthases are membrane-embedded glycosyltransferases. BcsB is a periplasmic protein that is anchored to the inner membrane via a single, C-terminal transmembrane helix. BcsA and BcsB are fused
-
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associated, the membrane-associated domain of BcsB is required for cellulose synthesis
-
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transmembrane structure, the catalytic site of cellulose synthase faces the cytosol, two polypeptides with their catalytic sites juxtapose to form a functional enzyme unit solving the problem of having to rotate the chain by 180° after each glucosyl residue addition, overview
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transmembrane structure, the catalytic site of cellulose synthase faces the cytosol, two polypeptides with their catalytic sites juxtapose to form a functional enzyme unit solving the problem of having to rotate the chain by 180° after each glucosyl residue addition, overview
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transmembrane structure, the catalytic site of cellulose synthase faces the cytosol, two polypeptides with their catalytic sites juxtapose to form a functional enzyme unit solving the problem of having to rotate the chain by 180° after each glucosyl residue addition, overview
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
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
dimer
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BcsA and BcsB form a 1:1 stoichiometric complex spanning approximately 150 A perpendicular and 55 A parallel to the membrane. The complex is divided into a cuboid-shaped membrane-spanning region sandwiched between large cytoplasmic and periplasmic domains. BcsA contains four N-terminal and four C-terminal transmembrane-helices separated by a large intracellular loop (4/5-loop) that forms a GT-domain (aa 128 to 368). transmembrane domains 3-8 form a narrow channel for the translocating polysaccharide and BcsA's intracellular C-terminus (aa 575 to 759) contains a 6-stranded beta-barrel and a highly curved alpha-helical region that attaches the beta-barrel to the GT-domain. BcsB is a dome-shaped, beta-strand rich, periplasmic protein. Its N-terminal region forms the tip of the dome, whereas the C-terminal transmembrane-anchor interacts with BcsA. Two amphipathic helices further stabilize its interaction with BcsA and the periplasmic water-membrane interface. Domain structures. Modeling, overview
additional information
existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position; existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position
additional information
existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position; existence of binding sites for three distinct CESA subunits in primary wall cellulose synthase complexes, with two positions being invariably occupied by CESA1 and CESA3, whereas at least three isoforms compete for the third position
additional information
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
additional information
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
additional information
secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers; secondary CESA proteins are organized in the rosette structure. Although all CESA proteins can interact with each other, only CESA4 is able to form homodimers
additional information
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cellulose synthase A is a catalytic component of the cellulose synthase complex. Mass spectrometric analysis of purified cellulose synthase components, His- and STREP-tagged CESA4, CESA7, and CESA8 from irx1-1, irx3-1, and irx5-2 mutant plants, overview
additional information
CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains; CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains
additional information
CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains; CesA isozymes all contains the D,D,D,QXXRW signature, their N-terminal ends exhibited oomycete-specific domains, i.e. Pleckstrin homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains
additional information
SpCesa1 contains an N-terminal cysteine-rich zinc binding domain, seven putative transmembrane helices, four U-motifs containing the conserved siganture DDDQXXRW, 1 conserved and two hypervariable regions
additional information
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two CesA enzymes, Csr2 and Csr4, are located in the same cellulose synthase enzyme complex
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
AtCesA7 is phosphorylated in vivo at two serine residues in a region of hyper-variability between the cellulose synthase catalytic subunits. Full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solution X-ray scattering of monomeric and dimeric catalytic subunits with or without bound substrate UDP-glucose
purified recombinant native and selenomethionine -labeled complex of BcsA and BcsB containing a translocating polysaccharide, from 30% PEG 200, 0.1 M MES, pH 6.5, and 50 mM NaCl at 4°C, 7 days, X-ray diffraction structure determination and analysis, modeling, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
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after 16 h more than half of activity of the solubilized form is lost
25
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after 1 h more than half of activity of the solubilized form is lost
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
full length endogenous CesA7 is degraded via a proteasome dependant pathway in whole plant extracts. Phosphorylation of the catalytic subunits may target them for degradation via a proteasome dependant pathway. This is a possible mechanism by which plants regulate the relative levels of the three proteins whose specific interaction are required to form an active cellulose synthase complex
when the protein is boiled in lithium dodecyl sulfate there is no detection of the 83000 Da polypeptide on the polyacrylamide gel, so the sample has to be incubated on ice
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1% digitonin, solubilized enzyme is stable for at least several h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IRX3 ist tightly bound to the cell wall and can only be released using very harsh conditions. Triton X-100 and NP40 are most effective. No effect: Triton X-114, Tween 80, Brij 35, Brij 58, CHAPS, octyl beta-glucoside, octyl beta-thioglucopyranoside
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native oligomers partially from microsomes as fragments of the cellulose synthase complex by dual epitope tagging of the CESA7 protein, selection for CESA multimers, overview. Recombinant His- and STREP-tagged CESA4, CESA7, and CESA8, as well as double mutant irx3-1:STREP-CESA7-irx3-1:His/FLAG-CESA7 from Arabidopsis thaliana irx1-1, irx3-1, and irx5-2 mutant plants by nickel and streptavidin affinity chromatography
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recombinant His-tagged native and selenomethionine -labeled subunits BcsA and B from Escherichia coli strain C43 by nickel affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CesA and Csl genes, detailed phylogenetic analysis, overview
CesA2, expression in Escherichia coli strain BL21(DE3) and in human U2OS osteosarcoma cells as GFP-tagged enzyme using the pCDNA6.2/GW/C-EmGFP vector
construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
expression of a PtCesAP-GUS fusion protein in Agrobacterium tumefaciens C58/pMP90; expression of DNA in lambda phage
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expression of His- and STREP-tagged CESA4, CESA7, and CESA8 in Arabidopsis thaliana using the Agrobacterium tumefaciens transfection nethod in the mutant lines are irx1-1, irx3-1, and irx5-2
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gene cesA, genotyping, quantitative real-time PCR assays, overview
gene cesA2, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis; gene cesA4, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
gene EgraCesA1, DNA and amino acid sequence determination and analysis, gene structure and genomic organization; gene EgraCesA1, DNA and amino acid sequence determination and analysis, gene structure and genomic organization; gene EgraCesA2, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA2 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview; gene EgraCesA2, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA2 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview; gene EgraCesA3, DNA and amino acid sequence determination and analysis, gene expression directed by the EgraCesA3 promoter or its deletions reveal several negative and positive regulatory regions controlling gene expression in xylem or phloem, a region is likely to contain mechanical stress-responsive elements, gene structure and genomic organization, overview
gene SpCesa1, from developing xylem, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
genes cslF and cslH, native expression under the control of a constitutive promoter, recombinant expression of Hordeum vulgare CslH gene in Arabidopsis thaliana leads to the deposition of mixed-linked beta-glucan in the cell wall, which do not contains this polysaccharide in Arabidopsis thaliana
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genes cslF and cslH, native expression under the control of a constitutive promoter, the genome contains a cluster of rice CslF genes, recombinant expression of Oryza sativa CslF genes in Arabidopsis thaliana leads to the deposition of mixed-linked beta-glucan in the cell wall, which do not contains this polysaccharide in Arabidopsis thaliana
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genes csr2 and csr4, quantitative real-time RT-PCR assays with four CesA gene transcripts, CesA1, 2, 3, and 4, in the wild-type genetic background, and on the two antisense CesA gene transcripts, CesA2 and 4. The two CesA genes show different expression patterns in tubers, overview
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interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview; interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview; interaction analysis between membrane-bound cellulose synthases using the yeast two-hybrid expression system in strain NMY51, confirmed by in planta by bimolecular fluorescence complementation assay, overview
recombinant expression of His-tagged subunits BcsA and B in Escherichia coli strain C43
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recombinant expression of subunits BcsA and B in Escherichia coli strain C43
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usage of the CesA enzyme family from Arabidopsis thaliana for construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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construction of a phylogeny-based CesA nomenclature for the Populus CesA gene family, aligning it with the enzyme family from Arabidopsis thaliana, phylogenetic analysis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CesA inhibition by 2,6-dichlorobenzonitrile or Congo Red results in increased expression of all CesA genes, overview; CesA inhibition by 2,6-dichlorobenzonitrile or Congo Red results in increased expression of all CesA genes, overview
EgraCesA1 gene expression is not upregulated in tension-stressed eucalyptus xylem cells, transcriptional regulation mechanisms of each EgraCesA genes, overview; EgraCesA1 gene expression is not upregulated in tension-stressed eucalyptus xylem cells, transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview; transcriptional regulation mechanisms of each EgraCesA genes, overview
EgraCesA2 gene expression is upregulated in tension-stressed eucalyptus xylem cells; EgraCesA2 gene expression is upregulated in tension-stressed eucalyptus xylem cells; EgraCesA3 gene expression is upregulated in tension-stressed eucalyptus xylem cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G998B
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
T942I
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
G998B
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
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T942I
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stable to the inhibitors: isoxaben and 5-tert-butyl-carbamoyloxy-3-(3-trifluormethyl)phenyl-4-thiazolidinone
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C37A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C37A/C56A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C37A/C64A C37A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C56A/C64A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C56A/C79A C64A/C79A
site-directed mutagenesis of the RING-motif leading to decreased interaction with other CESA proteins, overview
C64A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
C79A
site-directed mutagenesis of the RING-motif leading to slightly decreased interaction with other CESA proteins, overview
P578S
identification of thanatos, a semidominant mutant of Arabidopsis thaliana with impaired growth of seedlings due to a mutation in the catalytic domain of cellulose synthase 3, homozygous seedlings of than germinate and grow but do not survive, while heterozygous plants are dwarfed and display a radially swollen root phenotype, cellulose content is reduced by approximately one-fifth in heterozygous and by two-fifths in homozygous plants, overview. Gene dosage-dependent expression of the AtCesA3 mutant gene in wild-type Arabidopsis thaliana plants results in a than dominant-negative phenotype. The mutation alters the structure of the CESA3 catalytic domain
additional information
additional information
-
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. Cellulose contents of mutant lines irx5 and irx1 plants recombinantly expressing CESA8 and CESA4, irx5-2:STREP-CESA4 and irx1-1:STREPCESA8, are much lower than wild-type and as such are not fully functional. Recombinant mutant irx3-1 plants expressing STREP-CESA7 and His/FLAGCESA7 in a dual tag system have wild-type cellulose content and xylem phenotypes, overview. irx3-1:STREP-CESA7-irx3-1:His/FLAG-CESA7 crossed plants phenotype, overview
additional information
entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview
additional information
entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview
additional information
entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview
additional information
entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview
additional information
entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview; entire or deleted EgraCesA promoter::GUS reporter gene chimeras are constructed and introduced into Nicotiana tabacum using the Agrobacterium tumefaciens-mediated leaf disc transformation method, expression analysis, regulation, overview
additional information
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recombinant expression of genes csr2 and csr4in antisense orientation in transgenic Solanum tuberosum lines csr21 and csr48, and as double transformants. Medium-level downregulation of the CesA2 mRNA is observed in the csr2 tubers, but phenotypes may more likely be the result of downregulation of other CesA genes by siRNAs and not the result of downregulation of CesA2, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
antibodies against cotton Gossypium hirsutum Ces A3 are used to identify and localize Ces A proteins in Micrasterias denticulata
analysis
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antibodies against cotton Gossypium hirsutum Ces A3 are used to identify and localize Ces A proteins in Micrasterias denticulata
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.12)
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