| IED ID | IndEnz0005000586 |
| Enzyme Type ID | lipase000586 |
| Protein Name |
Acetylxylan esterase EC 3.1.1.72 Acetyl-xylooligosaccharide esterase |
| Gene Name | axe2 |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MKIGSGEKLLFIGDSITDCGRARPEGEGSFGALGTGYVAYVVGLLQAVYPELGIRVVNKGISGNTVRDLKARWEEDVIAQKPDWVSIMIGINDVWRQYDLPFMKEKHVYLDEYEATLRSLVLETKPLVKGIILMTPFYIEGNEQDPMRRTMDQYGRVVKQIAEETNSLFVDTQAAFNEVLKTLYPAALAWDRVHPSVAGHMILARAFLREIGFEWVRSR |
| Enzyme Length | 219 |
| Uniprot Accession Number | Q09LX1 |
| Absorption | |
| Active Site | ACT_SITE 15; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461"; ACT_SITE 191; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461"; ACT_SITE 194; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461" |
| 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:21994937}; |
| DNA Binding | |
| EC Number | 3.1.1.72 |
| Enzyme Function | FUNCTION: Acetylxylan esterase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Cleaves acetyl side groups from the xylose backbone units of the hemicellulolytic polymer xylan and xylo-oligosaccharides. Hydrolyzes about 20%-30% of the available acetyl groups on fully acetylated birch wood xylan. Completely deacetylates xylobiose peracetate (fully acetylated), and is active on both the alpha- and beta-forms of the sugar. Also hydrolyzes fully acetylated methyl-beta-D-xylopyranoside and methyl-beta-D-glucopyranoside, and the synthetic substrates 2-naphthyl acetate, 4-nitrophenyl acetate, 4-methylumbelliferyl acetate, and phenyl acetate. {ECO:0000269|PubMed:21994937}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50-60 degrees Celsius. Is stable at 60 degrees Celsius and loses most of its activity at 70 degrees Celsius. {ECO:0000269|PubMed:21994937}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.1-9.2. {ECO:0000269|PubMed:21994937}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000269|PubMed:21994937}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (7); Chain (1); Helix (14); Mutagenesis (5); Site (2); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cytoplasm;Hydrolase;Polysaccharide degradation;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Up-regulated by xylose. {ECO:0000269|PubMed:21994937}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21994937}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 3W7V; 4JHL; 4JJ4; 4JJ6; 4JKO; 4OAO; 4OAP; 5BN1; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,772 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 mM for phenyl acetate (at pH 6.0 and 30 degrees Celsius) {ECO:0000269|PubMed:21994937}; KM=9 mM for 2-naphtyl acetate (at pH 6.0 and 30 degrees Celsius) {ECO:0000269|PubMed:21994937}; KM=3 mM for 4-methylumbelliferyl acetate (at pH 6.0 and 30 degrees Celsius) {ECO:0000269|PubMed:21994937}; KM=27 mM for 4-nitrophenyl acetate (at pH 6.0 and 30 degrees Celsius) {ECO:0000269|PubMed:21994937}; Note=kcat is 77 sec(-1) with phenyl acetate as substrate. kcat is 190 sec(-1) with 2-naphtyl acetate as substrate. kcat is 123 sec(-1) with 4-methylumbelliferyl acetate as substrate. kcat is 31 sec(-1) with 4-nitrophenyl acetate as substrate (at pH 6.0 and 30 degrees Celsius). {ECO:0000269|PubMed:21994937}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.72; |