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Information on EC 3.1.1.58 - N-acetylgalactosaminoglycan deacetylase and Organism(s) Escherichia coli and UniProt Accession P75906
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3.1.1.58 N-acetylgalactosaminoglycan deacetylaseSpecify your search results
Word Map
- 3.1.1.58
- glycosylphosphatidylinositol
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deacetylases
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de-n-acetylation
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glcnac-pi
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chitin-binding
- drug development
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
de-n-acetylase, polysaccharide deacetylase, pnag de-n-acetylase, n-acetyl galactosaminoglycan deacetylase, bc0361, ba0150, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PgaB
encoded within pgaABCD operon, BLAST analyses: contains polysaccharide N-deacetylase domain of carbohydrate esterase 4 (CE4) family
deacetylase, polysaccharide
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N-acetyl galactosaminoglycan deacetylase
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PgaA
encoded within pgaABCD operon, BLAST analyses: not related to a protein of known function
polysaccharide deacetylase
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Vi-polysaccharide deacetylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-D-galactosaminoglycan acetylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY
52410-59-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O
acetate + ?
beta-1,6-GlcNAc (PGA) also called polysaccharide intracellular adhesin (PIA)
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?
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O
N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate
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the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers
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?
additional information
?
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deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
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?
additional information
?
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deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
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?
additional information
?
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involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
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?
additional information
?
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involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation
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?
additional information
?
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development of a fluorogenic assay to monitor the enzyme activity in vitro, overview. Monosaccharides are not substrates of the enzyme
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetylated beta-(1->6)-N-acetylglucosamine polymer + H2O
N-deacetylated beta-(1->6)-N-acetylglucosamine polymer + acetate
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the enzyme produces partially de-N-acetylated beta-(1->6)-N-acetylglucosamine polymers
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?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
-
-
?
additional information
?
-
deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzymes C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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methyl 2-deoxy-2-(sulfamoylamino)-beta-D-glucopyranoside
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9% inhibition at 1 mM
methyl 2-deoxy-2-[(hydroxyacetyl)(methyl)amino]-beta-D-glucopyranoside
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84% inhibition at 1 mM
methyl 2-deoxy-2-[(hydroxyacetyl)amino]-beta-D-glucopyranoside
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8% inhibition at 1 mM
methyl 2-deoxy-2-[(methylsulfonyl)amino]-beta-D-glucopyranoside
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7% inhibition at 1 mM
methyl 2-deoxy-2-[methyl(methylsulfonyl)amino]-beta-D-glucopyranoside
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18% inhibition at 1 mM
methyl 2-deoxy-2-[methyl(sulfamoyl)amino]-beta-D-glucopyranoside
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67% inhibition at 1 mM
methyl 2-deoxy-2-[methyl(sulfanylacetyl)amino]-beta-D-glucopyranoside
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48% inhibition at 1 mM
additional information
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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pH and temperature not specified in the publication
0.32
methyl 2-deoxy-2-[(hydroxyacetyl)(methyl)amino]-beta-D-glucopyranoside
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pH and temperature not specified in the publication
0.48
methyl 2-deoxy-2-[(sulfanylacetyl)amino]-beta-D-glucopyranoside
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pH and temperature not specified in the publication
5.8
methyl 2-deoxy-2-[methyl(methylsulfonyl)amino]-beta-D-glucopyranoside
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pH and temperature not specified in the publication
0.68
methyl 2-deoxy-2-[methyl(sulfamoyl)amino]-beta-D-glucopyranoside
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pH and temperature not specified in the publication
0.92
methyl 2-deoxy-2-[methyl(sulfanylacetyl)amino]-beta-D-glucopyranoside
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pH and temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
predicted, N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA) by PgaB promotes its export from periplasma by PgaA, defective PGA secretion in PgaB-deficient mutant strain
predicted beta-barrel porin of PgaA that forms outer membrane secretin for poly-beta-1,6-N-acetyl-D-glucosamine (PGA) and promotes its export from periplasm in response to N-deacetylation by PgaB, defective PGA secretion in PgaA-deficient mutant strain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the enzyme belongs to the the carbohydrate esterase family 4, CE4
physiological function
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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
additional information
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the enzyme has a His-His-Asp metal coordinating triad as well as conserved catalytic residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alignment with PDB database: hits to tetratricopeptide repeat domains of human nucleoporin O-linked N-acetylglucosamine transferase, yeast mitochondrial outer membrane translocon protein Tom70p, and human peroxisomal targeting signal-1 receptor PEX5, putative domains: porin domain for export of poly-beta-1,6-N-acetyl-D-glucosamine, and periplasmic domain for protein-protein interactions
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D115A
decreased catalytic activity, 6.4% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
PgaB271
DUF187 domain truncation mutant, amino acids 1-271, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 4.1% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin
PgaB410
DUF187 domain truncation mutant, amino acids 1-410, proteolytic cleavage during overexpression
PgaB516
DUF187 domain truncation mutant, amino acids 1-516, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 5% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin, proteolytic cleavage during overexpression
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
increased temperature might improve poly-beta-1,6-N-acetyl-D-glucosamine export in absence of deacetylation by PgaB
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of DUF187 domain truncation mutants PgaB516 and PgaB410 during overexpression in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from chromosomal DNA in pUC19 and subsequently in pCR2.1-TOPO for site directed mutagenesis and complementation experiments
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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the enzyme is a good target for therapeutic intervention in biofilm related infections
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, Y.; Rice, J.D.; Goller, C.; Pannuri, A.; Taylor, J.; Meisner, J.; Beveridge, T.J.; Preston, J.F.; Romeo, T.
Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine
J. Bacteriol.
190
3670-3680
2008
Escherichia coli (P69434), Escherichia coli (P75906), Escherichia coli K-12 MG1655 (P69434), Escherichia coli K-12 MG1655 (P75906)
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