Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a good target for therapeutic intervention in biofilm related infections | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
methyl 2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(octanoylsulfanyl)acetyl]amino]-beta-D-lucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside | - |
Escherichia coli | |
methyl 2-deoxy-2-(sulfamoylamino)-beta-D-glucopyranoside | 9% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[(hydroxyacetyl)(methyl)amino]-beta-D-glucopyranoside | 84% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[(hydroxyacetyl)amino]-beta-D-glucopyranoside | 8% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[(methylsulfonyl)amino]-beta-D-glucopyranoside | 7% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[(sulfanylacetyl)amino]-beta-D-glucopyranoside | - |
Escherichia coli | |
methyl 2-deoxy-2-[methyl(methylsulfonyl)amino]-beta-D-glucopyranoside | 18% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[methyl(sulfamoyl)amino]-beta-D-glucopyranoside | 67% inhibition at 1 mM | Escherichia coli | |
methyl 2-deoxy-2-[methyl(sulfanylacetyl)amino]-beta-D-glucopyranoside | 48% inhibition at 1 mM | Escherichia coli | |
additional information | synthesis and evaluation of a series of enzyme inhibitors, consisting of a metal chelating functional group on a glucosamine scaffold to target the active site metal ion of the enzyme, overview. No or poor inhibitory effect by methyl 2-deoxy-2-(glycylamino)-beta-D-glucopyranoside, methyl 2-deoxy-2-[(hydroxycarbamoyl)amino]-beta-D-glucopyranoside, methyl 2-deoxy-2-[glycyl(methyl)amino]-beta-D-glucopyranoside, and methyl 2-deoxy-2-[(hydroxycarbamoyl)(methyl)amino]-beta-D-glucopyranoside | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates | Escherichia coli | |
Fe2+ | activates | Escherichia coli | |
additional information | the enzyme requires an active site metal ion for activity. The enzyme from Escherichia coli has unique metal dependence, showing optimal activity with Fe2+, Ni2+, and Co2+ in contrast to the Zn2+ dependency observed for other N-deacetylases in the CE4 family | Escherichia coli | |
Ni2+ | activates | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O | Escherichia coli | the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers | N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene pgaB | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | development of a fluorogenic assay to monitor the enzyme activity in vitro, overview. Monosaccharides are not substrates of the enzyme | Escherichia coli | ? | - |
? | |
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O | the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers | Escherichia coli | N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PgaB | - |
Escherichia coli |
polysaccharide de-N-acetylase | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.28 | - |
methyl 2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(octanoylsulfanyl)acetyl]amino]-beta-D-lucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->6)-2-(acetylamino)-2-deoxy-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli | |
0.32 | - |
methyl 2-deoxy-2-[(hydroxyacetyl)(methyl)amino]-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli | |
0.48 | - |
methyl 2-deoxy-2-[(sulfanylacetyl)amino]-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli | |
0.68 | - |
methyl 2-deoxy-2-[methyl(sulfamoyl)amino]-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli | |
0.92 | - |
methyl 2-deoxy-2-[methyl(sulfanylacetyl)amino]-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli | |
5.8 | - |
methyl 2-deoxy-2-[methyl(methylsulfonyl)amino]-beta-D-glucopyranoside | pH and temperature not specified in the publication | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the the carbohydrate esterase family 4, CE4 | Escherichia coli |
additional information | the enzyme has a His-His-Asp metal coordinating triad as well as conserved catalytic residues | Escherichia coli |
physiological function | many medically important biofilm forming bacteria produce similar polysaccharide intercellular adhesins consisting of partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers, in Escherichia coli, de-N-acetylation of the beta-(1->6)-N-acetylglucosamine polymer is catalysed by deacetylase PgaB. N-Deacetylation of the polymers is essential for productive partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymer-dependent biofilm formation | Escherichia coli |