| IED ID | IndEnz0010001257 |
| Enzyme Type ID | esterase001257 |
| Protein Name |
Carbohydrate esterase MZ0003 EC 3.1.1.- |
| Gene Name | MZ0003 |
| Organism | Unknown prokaryotic organism |
| Taxonomic Lineage | cellular organisms Bacteria environmental samples Unknown prokaryotic organism |
| Enzyme Sequence | MQRTCVLIVLIVTSTMWTPDPDVYAQPRGFNYDEAQVPKYTLPDPLVMVDGTKVTSAKQWNDKRRDEVQQLFEAYMYGKVPDGETELIFTDAKGERALGGAAIRKQVKISFGEKEDAPAMDLLIYLPADAKVRVPVFLGLNFHGNHTIHKDKEIWLTESWVRTNKKFGITKNKANELSRGVAAGRWQIEKAIAKGYGVATIYCGDIDPDFNFPSNGIQAYYYKKDQTIPEKGQWGTIAAWAFGLSCAMDYFETDTDIDHKKVAVLGHSRLGKTSLWAGAIDTRFALTISNCSGCGGAALSRRRFGETVRRINTSFPHWFCSRFHQYNDKEDKLPIDQHMLIALCAPRPVLINSATEDKWADPHGEFLAAQGADAVYRMLGTGGLDAKKWPEPNKLVKSTIGYHLRPGKHDVTARDWDVYIEFADHHMTGGAE |
| Enzyme Length | 432 |
| Uniprot Accession Number | A0A0K2VM55 |
| Absorption | |
| Active Site | ACT_SITE 268; /note=Nucleophile; /evidence=ECO:0000305|PubMed:27433797; ACT_SITE 409; /note=Charge relay system; /evidence=ECO:0000305|PubMed:27433797 |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited by PMSF and by NaF in vitro, which is consistent with the catalytic nucleophile being a serine. {ECO:0000269|PubMed:27433797}. |
| Binding Site | BINDING 272; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6; BINDING 359; /note=Substrate; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Displays some glucuronoyl esterase activity in vitro, since it is able to hydrolyze methyl 4-O-methyl-D-glucopyranosyluronate, allyl D-glucuronate, benzyl D-glucuronate and D-glucuronic acid methyl ester. However, esters of glucuronic acid are probably not its biological substrate, as they are not present in the marine environment. Can also hydrolyze a range of other esters, including p-nitrophenyl acetate. More likely biologically-relevant substrates for MZ0003 and other marine bacterial CE15s are algal cell wall polysaccharides, as these would be readily available in this environment and could be used as energy sources. {ECO:0000269|PubMed:27433797}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius with p-nitrophenyl acetate as substrate. Above 35 degrees Celsius, activity significantly decreases, while 30% of the maximum activity is recorded at 10 degrees Celsius. {ECO:0000269|PubMed:27433797}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Shows more than 60% of its maximum activity in the pH range of 7.0-9.5. 20% of the activity is retained at low pH range and at pH 10.5, while no catalytic activity is found at pH 5.0 or 10.5. {ECO:0000269|PubMed:27433797}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Binding site (2); Chain (1); Helix (22); Motif (1); Mutagenesis (4); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Carbohydrate metabolism;Hydrolase;Periplasm;Polysaccharide degradation;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:27433797}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6EHN; |
| Mapped Pubmed ID | 29222424; |
| Motif | MOTIF 266..271; /note=GXSYXG catalytic site motif; /evidence=ECO:0000250|UniProtKB:G2QJR6 |
| Gene Encoded By | |
| Mass | 48,457 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.71 mM for p-nitrophenyl acetate (in the absence of NaCl) {ECO:0000269|PubMed:27433797}; KM=0.97 mM for p-nitrophenyl acetate (in the presence of 1M NaCl) {ECO:0000269|PubMed:27433797}; Note=kcat is 8.9 sec(-1) with p-nitrophenyl acetate as substrate (in the absence of NaCl). kcat is 12.78 sec(-1) with p-nitrophenyl acetate as substrate (in the presence of 1M NaCl). {ECO:0000269|PubMed:27433797}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |