Detail Information for IndEnz0002001993
IED ID IndEnz0002001993
Enzyme Type ID protease001993
Protein Name Crustapain
EC 3.4.22.-
NsCys
Gene Name Cys
Organism Pandalus borealis (Northern red shrimp)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Crustacea Multicrustacea Malacostraca Eumalacostraca Eucarida Decapoda Pleocyemata Caridea Pandaloidea Pandalidae (pandalid shrimps) Pandalus Pandalus borealis (Northern red shrimp)
Enzyme Sequence MRSLFLILLGLAAVSAIGEWENFKTKFGKKYANSEEESHRMSVFMDKLKFIQEHNERYDKGEVTYWLKINNFSDLTHEEVLATKTGMTRRRHPLSVLPKSAPTTPMAADVDWRNKGAVTPVKDQGQCGSCWAFSAVAALEGAHFLKTGDLVSLSEQNLVDCSSSYGNQGCNGGWPYQAYQYIIANRGIDTESSYPYKAIDDNCRYDAGNIGATVSSYVEPASGDESALQHAVQNEGPVSVCIDAGQSSFGSYGGGVYYEPNCDSWYANHAVTAVGYGTDANGGDYWIVKNSWGAWWGESGYIKMARNRDNNCAIATYSVYPVV
Enzyme Length 323
Uniprot Accession Number Q86GF7
Absorption
Active Site ACT_SITE 130; /evidence=ECO:0000250|UniProtKB:P07711; ACT_SITE 269; /evidence=ECO:0000250|UniProtKB:P07711; ACT_SITE 290; /evidence=ECO:0000250|UniProtKB:P07711
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.22.-
Enzyme Function FUNCTION: Cysteine protease which may be involved in digestion. Shows highest affinity for proline at the P2 position. Cleaves valine more efficiently than leucine and exhibits 10-fold lower affinity for phenylalanine than proline. Can cleave type I collagen. {ECO:0000269|PubMed:12869537}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius but displays considerable activity as low as 20 degrees Celsius. Thermostable. Retains 60% of initial activity after incubation at 50 degrees Celsius for 2 hours. {ECO:0000269|PubMed:12869537};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. Unstable at pH values less than 5.0 and remains fully active over a wide alkaline pH range. {ECO:0000269|PubMed:12869537};
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (3); Propeptide (1); Signal peptide (1)
Keywords Collagen degradation;Digestion;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Signal;Thiol protease;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 35,525
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=118 uM for Z-Phe-Arg-MCA (at pH 4.0) {ECO:0000269|PubMed:12869537}; KM=78 uM for Z-Phe-Arg-MCA (at pH 6.0) {ECO:0000269|PubMed:12869537}; KM=86 uM for Z-Phe-Arg-MCA (at pH 8.0) {ECO:0000269|PubMed:12869537}; KM=98 uM for Z Pro-Arg-MCA (at pH 4.0) {ECO:0000269|PubMed:12869537}; KM=65 uM for Z-Pro-Arg-MCA (at pH 6.0) {ECO:0000269|PubMed:12869537}; KM=70 uM for Z-Pro-Arg-MCA (at pH 8.0) {ECO:0000269|PubMed:12869537};
Metal Binding
Rhea ID
Cross Reference Brenda