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Literature summary extracted from

  • Munan Shaik, M.; Bhattacharjee, N.; Bhattacharjee, A.; Field, M.; Zanotti, G.
    Characterization of the divalent metal binding site of bacterial polysaccharide deacetylase using crystallography and quantum chemical calculations (2014), Proteins, 82, 1311-1318.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.104 gene hp0310, expression as N-terminally His6-tagged enzyme Helicobacter pylori
3.5.1.104 gene hp0310, sequence comparison, recombinant expression of N-terminally His6-tagged enzyme Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.104 purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution Helicobacter pylori
3.5.1.104 purified recombinant N-terminally His6-tagged enzyme, vapor diffusion technique, mixing of 18 mg/ml protein solution with precipitant solution containing 0.2 M ammonium sulfate, 0.1 M tris sodium citrate, pH 5.6, and 15% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement and modeling Helicobacter pylori

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.104 EDTA complete inhibition Helicobacter pylori

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.104 additional information metal site models show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur, e.g. Fe2+, Co2+, Cu2+, Mg2+, quantum chemical calculations, overview Helicobacter pylori
3.5.1.104 Zn2+ the zinc ion of the metalloenzyme is coordinated by a conserved binding triad of amino acids consisting of one aspartate and two histidine residues, determination of the metal-binding site, which is essential for the enzyme's catalytic activity, one metal site per monomer, structure and quantum chemical calculations of models, overview. The metal ion occupies a tetrahedral environment with binding to one of the carboxylic oxygen of Asp14, His86, His90 and a water molecule Helicobacter pylori
3.5.1.104 Zn2+ divalent metal binding site, one site per enzyme monomer, essential for the enzyme's catalytic activity, structure analysis, detailed overview Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O Helicobacter pylori
-
 peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O Helicobacter pylori the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O Helicobacter pylori G27
-
 peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O Helicobacter pylori G27 the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria peptidoglycan-D-glucosamine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.104 Helicobacter pylori B5ZA76 gene pgdA or hp0310
-
3.5.1.104 Helicobacter pylori B5ZA76 gene hp0310
-
3.5.1.104 Helicobacter pylori G27 B5ZA76 gene hp0310
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.104 recombinant N-terminally His6-tagged enzyme Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O
-
 Helicobacter pylori peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria Helicobacter pylori peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O
-
 Helicobacter pylori G27 peptidoglycan-D-glucosamine + acetate
-
 ?
3.5.1.104 peptidoglycan-N-acetyl-D-glucosamine + H2O the enzyme catalyzes the removal of the acetyl group from the C2 atom of N-acetylglucosamine, which is a constituent of the peptidoglycan found in the cell walls of many bacteria Helicobacter pylori G27 peptidoglycan-D-glucosamine + acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.104 homotetramer
-
 Helicobacter pylori
3.5.1.104 tetramer
-
 Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
3.5.1.104 HP0310
-
 Helicobacter pylori
3.5.1.104 HpPgdA
-
 Helicobacter pylori
3.5.1.104 peptidoglycan deacetlyase
-
 Helicobacter pylori
3.5.1.104 pgdA
-
 Helicobacter pylori
3.5.1.104 polysaccharide deacetylase
-
 Helicobacter pylori

General Information

EC Number General Information Comment Organism
3.5.1.104 physiological function the enzyme is responsible for a peptidoglycan modification that counteracts the host immune response Helicobacter pylori
3.5.1.104 physiological function peptidoglycan deacetylase is the enzyme responsible for a peptidoglycan modification that counteracts the host immune response Helicobacter pylori