Detail Information for IndEnz0002018805
IED ID IndEnz0002018805
Enzyme Type ID protease018805
Protein Name Isoaspartyl peptidase/L-asparaginase
EC 3.4.19.5
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase

Cleaved into: Isoaspartyl peptidase/L-asparaginase subunit alpha; Isoaspartyl peptidase/L-asparaginase subunit beta
Gene Name all3922
Organism Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Nostocales Nostocaceae Nostoc unclassified Nostoc Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Enzyme Sequence MKSQVQPKLIIHGGAGSSLHGKGGLEAVRQTLHAVVEEVYALLLSGVNASVAVVRGCQLLEDEPRFNAGTGSVLQSDGQIRMSASIMDGALGRFSGVINVSRVKNPIELAQFLQNSPDRVLSDYGSAELAREMQIPSYNALTELRLQEWIQERQDNFKRTMAGVIAEPELLETSNAGRGTIGVVALDTYGKLAVGTSTGGKGFERIGRVSDSAMPAGNYATSYAAVSCTGIGEDIIDECLAPKIVIRVTDGLSLQDSMQRSFAEAHDNKRDFGAIALDANGAIAWGKTCDIILAAFHDGEKIGDTLELAVGTQVGSIS
Enzyme Length 318
Uniprot Accession Number Q8YQB1
Absorption
Active Site ACT_SITE 180; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.; EC=3.4.19.5;
DNA Binding
EC Number 3.4.19.5
Enzyme Function FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Probably performs the final step in the degradation of the reserve polymer cyanophycin (depolymerizes the building block L-beta-Asp-Arg). Also has L-asparaginase activity. {ECO:0000269|PubMed:11988085}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (2); Region (2); Site (1)
Keywords Autocatalytic cleavage;Direct protein sequencing;Hydrolase;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,638
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.0 mM for L-Asn; KM=1.54 mM for L-beta-Asp-Ala; KM=0.27 mM for L-beta-Asp-Arg; KM=0.52 mM for L-beta-Asp-Gly; KM=0.26 mM for L-beta-Asp-Leu; KM=0.53 mM for L-beta-Asp-Lys; KM=0.68 mM for L-beta-Asp-Phe; Vmax=2.2 umol/min/mg enzyme with L-Asn as substrate; Vmax=12.3 umol/min/mg enzyme with L-beta-Asp-Ala as substrate; Vmax=5.7 umol/min/mg enzyme with L-beta-Asp-Arg as substrate; Vmax=2.7 umol/min/mg enzyme with L-beta-Asp-Gly as substrate; Vmax=4.5 umol/min/mg enzyme with L-beta-Asp-Leu as substrate; Vmax=22.2 umol/min/mg enzyme with L-beta-Asp-Lys as substrate; Vmax=20.1 umol/min/mg enzyme with L-beta-Asp-Phe as substrate; Note=Enzyme is inactive on alpha-aspartyl dipeptides.;
Metal Binding
Rhea ID
Cross Reference Brenda