Detail Information for IndEnz0010001102
IED ID IndEnz0010001102
Enzyme Type ID esterase001102
Protein Name Chitin deacetylase 8
BmCDA8
EC 3.5.1.41
Chitin deacetylase 17
Gene Name CDA8
Organism Bombyx mori (Silk moth)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Bombycidae (silkworm moths) Bombycinae Bombyx Bombyx mori (Silk moth)
Enzyme Sequence MKRLSVLCSLLLVAAALGTELPLATPCDEEACKLPDCRCSSTNIPGGLRARDTPQFVTVTFDDGINVINIETYREVLYGRSNSNRCPAGATFYVSHEYTNYQLVNELYNRGFEIALHSISHRTPQAFWADATYQNLVQEIGDQKRQMAHFASIPASAIKGVRIPFLQMSGNTSFQVMADFDLLYDCTWPTTALTNPGLWPYTLHHESIQDCIIPPCPTASIPGPWVLPMISWRDLNNFPCSMVDGCFFTPDRTDEEGWFKFILTNFERHYLGNRAPFGFFVHEWFISSNPAIKRAFVRFMDIINNLNDVFMVNSAEVIDWVKNPVPIDRYRQQQCKFTMPSICRPSFCGPLTGTHNQLSYYMTICNTCPRNYPWVGNPLGQ
Enzyme Length 381
Uniprot Accession Number H9JW43
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:30755482};
DNA Binding
EC Number 3.5.1.41
Enzyme Function FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine (GlcNAc) residues in chitin. Shows activity towards the chitinous oligomers GlcNAc(3), GlcNAc(4), GlcNAc(5) and GlcNAc(6), but not GlcNAc or GlcNAc(2). Requires the substrate to occupy subsites 0, +1, and +2 for optimum catalysis. {ECO:0000269|PubMed:30755482}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (7); Glycosylation (1); Metal binding (3); Mutagenesis (2); Signal peptide (1)
Keywords 3D-structure;Carbohydrate metabolism;Chitin degradation;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Polysaccharide degradation;Reference proteome;Secreted;Signal;Zinc
Interact With
Induction INDUCTION: Strongly down-regulated in response to 20-hydroxyecdysone (20E). Up-regulated in response to juvenile hormone analog. {ECO:0000269|PubMed:30987273}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5Z34;
Mapped Pubmed ID 29251378;
Motif
Gene Encoded By
Mass 43,310
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76.7 mM for GlcNAc(3) {ECO:0000269|PubMed:30755482}; KM=12.3 mM for GlcNAc(4) {ECO:0000269|PubMed:30755482}; KM=15.7 mM for GlcNAc(5) {ECO:0000269|PubMed:30755482}; KM=9.2 mM for GlcNAc(6) {ECO:0000269|PubMed:30755482}; KM=1.926 mg/ml for ethylene glycol chitin {ECO:0000269|PubMed:30755482}; KM=1.599 mg/ml for colloidal chitin {ECO:0000269|PubMed:30755482}; Note=kcat is 7.62 min(-1) for GlcNAc(3) (PubMed:30755482). kcat is 5.59 min(-1) for GlcNAc(4) (PubMed:30755482). kcat is 7.52 min(-1) for GlcNAc(5) (PubMed:30755482). kcat is 9.07 min(-1) for GlcNAc(6) (PubMed:30755482). kcat is 0.097 min(-1) for ethylene glycol chitin (PubMed:30755482). kcat is 0.012 min(-1) for colloidal chitin (PubMed:30755482). {ECO:0000269|PubMed:30755482};
Metal Binding METAL 63; /note="Zinc"; /evidence="ECO:0000269|PubMed:30755482, ECO:0007744|PDB:5Z34"; METAL 117; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30755482, ECO:0007744|PDB:5Z34"; METAL 121; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30755482, ECO:0007744|PDB:5Z34"
Rhea ID RHEA:10464
Cross Reference Brenda 3.5.1.41;