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