Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (PgaB)

Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (PgaB) is a periplasmic bacterial enzyme classified in the carbohydrate esterase family 4 (CE4)[1][3]. It participates in biofilm formation by catalyzing the partial de-N-acetylation of the exopolysaccharide PNAG, a modification required for strong intercellular adhesion and biofilm integrity in Escherichia coli and other Gram-negative bacteria[1][3][8]. Structurally, PgaB contains an N-terminal de-N-acetylase domain and a C-terminal domain involved in polymer binding and/or export, sometimes facilitated by interaction with other biofilm machinery proteins, such as PgaA[2]. The enzyme’s specificity and efficiency are governed by a unique active site and metal (Ni2+, Fe3+) coordination, and its function impacts bacterial survival and pathogenicity[1][2][3][8]. Targeting PgaB or its activity is of therapeutic interest in the context of anti-biofilm strategies for combating chronic bacterial infections[2].

Other names

Poly-β-1,6-N-acetyl-D-glucosamine N-deacetylasePNAG N-deacetylasePgaB (gene/protein name)