| IED ID | IndEnz0011000085 |
| Enzyme Type ID | glucanase000085 |
| Protein Name |
Glucan endo-1,3-beta-glucosidase EC 3.2.1.39 1- 3 -beta-glucan endohydrolase 1- 3 -beta-glucanase CaLam Endo-beta-1,3-glucanase Laminarinase |
| Gene Name | |
| Organism | Cryptopygus antarcticus (Antarctic springtail) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Collembola (springtails) Entomobryomorpha Isotomoidea Isotomidae (smooth springtails) Anurophorinae Cryptopygus Cryptopygus antarcticus complex Cryptopygus antarcticus (Antarctic springtail) |
| Enzyme Sequence | MNAFTFPLLLAFCAFAHGAWVLDWEDEFNGGNLADRWNFELGCNGWGNNELQCYTDNRGANARQEDGKLVISAVREWWGDGVNPDKEFTSARMTTKANWLHGKFEMRARLPKGKHLWPAFWMMPQNSEYGGWPRSGEIDITEYRGQRPQQILGTLHFGAAPDNKGDVGTGERDFPIDFSADFHTFGLDWSPDSMQWLLDDQVYHTESLQRNFWDGVYNQNGSPFDKNFFIILNLAVGGNFFGGEPFDPSESDGWAKNTFEVEYVKKWTWN |
| Enzyme Length | 270 |
| Uniprot Accession Number | C1IE32 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01098; ACT_SITE 142; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01098 |
| Activity Regulation | ACTIVITY REGULATION: Ca(2+) does not affect the enzyme activity nor the thermostability. Other cations, such as Mg(2+), Mn(2+), Cu(2+), Zn(2+), Ag(+) or Hg(2+) do not cause any serious adverse effect on the activity. Also no significant change in the activity in response to the addition of 1 mM EDTA. {ECO:0000269|PubMed:20079869}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:20079869}; |
| DNA Binding | |
| EC Number | 3.2.1.39 |
| Enzyme Function | FUNCTION: Hydrolyzes laminarin majorily to glucose (G1), laminaribiose (L2), laminaritriose (L3), laminaritetraose (L4) and laminaripentaose (L5). Hydrolyzes laminarioligosaccharides L3, L4, L5 and laminarihexaose (L6) to G1, L2 and L3. Hardly hydrolyzes L2. Does not hydrolyze lichenan, pustulan, carboxymethyl cellulose, locust bean gum or soluble starch. {ECO:0000269|PubMed:20079869}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Retains 20% of the maximal activity after incubation at 60 degrees Celsius for 30 min. Retains approximately 15% of the maximal activity at the temperature below 15 degrees Celsius. {ECO:0000269|PubMed:20079869}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. More than 80% of its maximal activity is maintained at pH 5.5-6.5. {ECO:0000269|PubMed:20079869}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Signal peptide (1) |
| Keywords | Glycosidase;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,008 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.98 mg/ml for 1% laminarin (at pH 6.0 and 50 degrees Celsius) {ECO:0000269|PubMed:20079869}; Vmax=32.2 umol/min/mg enzyme with 1% laminarin as substrate (at pH 6.0 and 50 degrees Celsius) {ECO:0000269|PubMed:20079869}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.39; |