BRENDA - Enzyme Database show

BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis

Omadjela, O.; Narahari, A.; Strumillo, J.; Melida, H.; Mazur, O.; Bulone, V.; Zimmer, J.; Proc. Natl. Acad. Sci. USA 110, 17856-17861 (2013)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.12
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
Rhodobacter sphaeroides
Cloned(Commentary)
EC Number
Commentary
Organism
2.4.1.12
recombinant expression of subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
General Stability
EC Number
General Stability
Organism
2.4.1.12
BcsA-B is catalytically active in a detergent-solubilized state
Rhodobacter sphaeroides
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.12
additional information
no inhibition by guanosine and adenosine diphosphates
Rhodobacter sphaeroides
2.4.1.12
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
Rhodobacter sphaeroides
2.4.1.12
UDP-alpha-D-xylose
strong inhibition
Rhodobacter sphaeroides
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.12
additional information
-
additional information
monophasic Michaelis-Menten kinetics, kinetic analysis of cellulose synthesis, overview
Rhodobacter sphaeroides
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.12
inner membrane
associated, the membrane-associated domain of BcsB is required for cellulose synthesis
Rhodobacter sphaeroides
-
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.12
Rhodobacter sphaeroides
Q3J125
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
737161
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.12
37
-
assay at
Rhodobacter sphaeroides
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.12
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
Rhodobacter sphaeroides
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.12
recombinant expression of subunits BcsA and B in Escherichia coli strain C43
Rhodobacter sphaeroides
General Stability (protein specific)
EC Number
General Stability
Organism
2.4.1.12
BcsA-B is catalytically active in a detergent-solubilized state
Rhodobacter sphaeroides
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.4.1.12
additional information
no inhibition by guanosine and adenosine diphosphates
Rhodobacter sphaeroides
2.4.1.12
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
Rhodobacter sphaeroides
2.4.1.12
UDP-alpha-D-xylose
strong inhibition
Rhodobacter sphaeroides
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4.1.12
additional information
-
additional information
monophasic Michaelis-Menten kinetics, kinetic analysis of cellulose synthesis, overview
Rhodobacter sphaeroides
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.12
inner membrane
associated, the membrane-associated domain of BcsB is required for cellulose synthesis
Rhodobacter sphaeroides
-
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
Rhodobacter sphaeroides
-
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.12
UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
737161
Rhodobacter sphaeroides
UDP + [(1->4)-beta-D-glucosyl]n+1
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.12
37
-
assay at
Rhodobacter sphaeroides
General Information
EC Number
General Information
Commentary
Organism
2.4.1.12
additional information
BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
Rhodobacter sphaeroides
2.4.1.12
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
Rhodobacter sphaeroides
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.4.1.12
additional information
BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
Rhodobacter sphaeroides
2.4.1.12
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
Rhodobacter sphaeroides