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Literature summary extracted from

  • Omadjela, O.; Narahari, A.; Strumillo, J.; Melida, H.; Mazur, O.; Bulone, V.; Zimmer, J.
    BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis (2013), Proc. Natl. Acad. Sci. USA, 110, 17856-17861.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment 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 Cereibacter sphaeroides

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.12 recombinant expression of subunits BcsA and B in Escherichia coli strain C43 Cereibacter sphaeroides

General Stability

EC Number General Stability Organism
2.4.1.12 BcsA-B is catalytically active in a detergent-solubilized state Cereibacter sphaeroides

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.12 additional information no inhibition by guanosine and adenosine diphosphates Cereibacter 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 Cereibacter sphaeroides
2.4.1.12 UDP-alpha-D-xylose strong inhibition Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.12 additional information
-
 additional information monophasic Michaelis-Menten kinetics, kinetic analysis of cellulose synthesis, overview Cereibacter sphaeroides

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.12 inner membrane associated, the membrane-associated domain of BcsB is required for cellulose synthesis Cereibacter sphaeroides
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.12 UDP-glucose + [(1->4)-beta-D-glucosyl]n Cereibacter sphaeroides
-
 UDP + [(1->4)-beta-D-glucosyl]n+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.12 Cereibacter sphaeroides Q3J125
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.12 UDP-glucose + [(1->4)-beta-D-glucosyl]n
-
 Cereibacter sphaeroides UDP + [(1->4)-beta-D-glucosyl]n+1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.12 BcsA-B
-
 Cereibacter sphaeroides
2.4.1.12 inner membrane-associated bacterial cellulose synthase
-
 Cereibacter sphaeroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.12 37
-
 assay at Cereibacter sphaeroides

General Information

EC Number General Information Comment 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 Cereibacter 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 Cereibacter sphaeroides