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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

Reaction

UDP-alpha-D-glucose
+
[(1->4)-beta-D-glucosyl]n
=
UDP
 +
[(1->4)-beta-D-glucosyl]n+1

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 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.12 cellulose synthase (UDP-forming)

Activating Compound

Activating Compound on EC 2.4.1.12 - cellulose synthase (UDP-forming)

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-cGMP
-
-
cellobiose
cellodextrins
-
stimulate cellulose synthesis, cellulose synthesis is dependent on presence of a soluble primer
cyclic diguanylate
-
allosteric activator, required for catalytic activity
Cyclic diguanylic acid
-
stimulation
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
D-glucose
-
1 M, 7fold stimulation
Digitonin
-
optimal concentration is 0.05%
methyl-beta-D-glucoside
-
1 M, 11fold stimulation
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
additional information
-