| IED ID | IndEnz0010001405 |
| Enzyme Type ID | esterase001405 |
| Protein Name |
Peptidoglycan deacetylase PG deacetylase EC 3.5.1.- Acetylxylan esterase EC 3.1.1.72 |
| Gene Name | pgdA HP_0310 C694_01565 |
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Enzyme Sequence | MAKEILVAYGVDIDAVAGWLGSYGGEDSPDDISRGLFAGEVGIPRLLKLFKKYHLPATWFSPGHSIETFSEQMKMIVDAGHEVGAHGYSHENPIAMTAKQEEDVLLKSVELIKDLTGKAPTGYVAPWWEFSNITNELLLKHGFKYDHSLMHNDFTPYYVRVGDSWSKIDYSLEAKDWMKPLIRGVETDLVEIPANWYLDDLPPMMFIKKSPNSFGFVSPHDIGQMWIDQFDWVYREMDYAVFSMTIHPDVSARPQVLLMHEKIIEHINKHEGVRWVTFNEIADDFLKRNPRKK |
| Enzyme Length | 293 |
| Uniprot Accession Number | O25080 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:23825549}; |
| DNA Binding | |
| EC Number | 3.5.1.-; 3.1.1.72 |
| Enzyme Function | FUNCTION: Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection; this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans. {ECO:0000269|PubMed:19147492, ECO:0000269|PubMed:20805339, ECO:0000269|PubMed:23221800, ECO:0000269|PubMed:23825549}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius with acetylated xylan as substrate. Retains about 80% of the activity at 30-55 degrees Celsius. {ECO:0000269|PubMed:23825549}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 with acetylated xylan as substrate. Is active at acidic pH ranging from 5.0 to 6.0. {ECO:0000269|PubMed:23825549}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Initiator methionine (1); Metal binding (3) |
| Keywords | Carbohydrate metabolism;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Stress response;Xylan degradation;Zinc |
| Interact With | |
| Induction | INDUCTION: Its expression is markedly up-regulated upon cell exposure to oxidative stress. Is also significantly induced (3.5-fold) when H.pylori cells are in contact with macrophages. {ECO:0000269|PubMed:19147492, ECO:0000269|PubMed:20805339}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,677 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.85 mM for chitin {ECO:0000269|PubMed:23825549}; KM=0.85 mM for chitosan {ECO:0000269|PubMed:23825549}; KM=0.42 mM for acetylated xylan {ECO:0000269|PubMed:23825549}; KM=0.18 mM for pNP-acetate {ECO:0000269|PubMed:23825549}; Note=kcat is 775 min(-1), 968 min(-1), 2549 min(-1) and 1029 min(-1) with chitin, chitosan, acetylated xylan, and pNP-acetate as substrate, respectively.; |
| Metal Binding | METAL 14; /note=Zinc; /evidence=ECO:0000250; METAL 86; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250; METAL 90; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.5.1.104; |