| IED ID | IndEnz0010001363 |
| Enzyme Type ID | esterase001363 |
| Protein Name |
Cephalosporin-C deacetylase EC 3.1.1.41 Acetylxylan esterase EC 3.1.1.72 |
| Gene Name | axeA TM_0077 |
| Organism | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga maritima Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Enzyme Sequence | MAFFDLPLEELKKYRPERYEEKDFDEFWEETLAESEKFPLDPVFERMESHLKTVEAYDVTFSGYRGQRIKGWLLVPKLEEEKLPCVVQYIGYNGGRGFPHDWLFWPSMGYICFVMDTRGQGSGWLKGDTPDYPEGPVDPQYPGFMTRGILDPRTYYYRRVFTDAVRAVEAAASFPQVDQERIVIAGGSQGGGIALAVSALSKKAKALLCDVPFLCHFRRAVQLVDTHPYAEITNFLKTHRDKEEIVFRTLSYFDGVNFAARAKIPALFSVGLMDNICPPSTVFAAYNYYAGPKEIRIYPYNNHEGGGSFQAVEQVKFLKKLFEKG |
| Enzyme Length | 325 |
| Uniprot Accession Number | Q9WXT2 |
| Absorption | |
| Active Site | ACT_SITE 188; /note=Nucleophile; /evidence=ECO:0000269|PubMed:22411095; ACT_SITE 274; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P94388; ACT_SITE 303; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P94388 |
| Activity Regulation | ACTIVITY REGULATION: Activity stimulated by up to 40% in the presence of divalent cations such as BaCl(2), CaCl(2), MgCl(2) and MnCl(2) at 3 mM concentration, but inhibited by 82-85% in the presence of CdCl(2) and ZnCl(2) at 3 mM concentration. {ECO:0000269|PubMed:21255309}. |
| Binding Site | BINDING 92; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P94388; BINDING 188; /note=Paraoxon; inhibitor; covalent; /evidence=ECO:0000269|PubMed:22411095 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; Evidence={ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095}; CATALYTIC ACTIVITY: Reaction=cephalosporin C + H2O = acetate + deacetylcephalosporin C + H(+); Xref=Rhea:RHEA:22596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57511, ChEBI:CHEBI:58366; EC=3.1.1.41; Evidence={ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095}; |
| DNA Binding | |
| EC Number | 3.1.1.41; 3.1.1.72 |
| Enzyme Function | FUNCTION: Esterase that removes acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylo-oligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan, 4-methylumbelliferyl acetate or alpha-naphthyl acetate. Able to catalyze rapid hydrolysis of a range of substrates preferably with acetate groups, independent of the alcohol moiety. Exhibits a narrow selectivity for short chain acyl esters (C2-C3). Displays broad substrate specificity by hydrolyzing acetate at 2, 3, and 4 positions of 4-nitrophenyl-beta-D-xylopyranoside (pNP-Xyl) with similar efficiency. Cannot cleave amide linkages. {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius. Activity drops sharply above 90 degrees Celsius. Stable up to 100-104 degrees Celsius. {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Half-maximal activity between pH 5.0-7.5. {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Binding site (2); Chain (1); Helix (14); Mutagenesis (9); Turn (3) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cellulose degradation;Cytoplasm;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P94388}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1VLQ; 3M81; 3M82; 3M83; 5FDF; 5GMA; 5HFN; 5JIB; |
| Mapped Pubmed ID | 27085421; 27181355; 28097692; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,156 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 mM for p-nitrophenyl-acetate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=6.05 mM for glucose penta-acetate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=4.18 mM for cephalosporin-C {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=20.8 mM for 7-aminocephalosporonic acid (7-ACA) {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=760 uM for p-nitrophenyl acetate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=3.7 uM for fluoroscein di(acetoxymethyl) ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.97 uM for fluoroscein dipropyloxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.41 uM for fluoroscein dibutyloxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=1.0 uM for fluoroscein divaleryloxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=2.6 uM for fluoroscein dicaproyloxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.51 uM for fluoroscein dimethacryloxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.96 uM for fluoroscein dicyclobutylcarboxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.54 uM for fluoroscein dimethylcyclopropanecarboxymethyl ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.185 mM for p-nitrophenyl-acetate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=0.137 mM for p-nitrophenyl-propionate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=3.6 mM for 2-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=4.2 mM for 3-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; KM=4.0 mM for 4-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; Vmax=113.5 umol/min/mg enzyme with pNP-acetate as substrate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; Vmax=366.8 umol/min/mg enzyme with glucose penta-acetate as substrate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; Vmax=19.2 umol/min/mg enzyme with cephalosporin-C as substrate {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; |
| Metal Binding | |
| Rhea ID | RHEA:22596 |
| Cross Reference Brenda | 3.1.1.41; |