UniProt functional annotation for P39377



	UniProt functional annotation for P39377

UniProt code: P39377.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu. {ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:4880759, ECO:0000269|PubMed:7876157}.

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050}; Note=Binds 2 Zn(2+) ions per subunit. Has highest activity with Zn(2+) ions, but is also active with Co(2+) ions. {ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050};

Activity regulation: P-hydroxymercuribenzoate causes a slight inhibition (8 to 17 %). Iodoacetamide, o-iodosobenzoate and ammonium persulfate do not inhibit the enzyme activity. {ECO:0000269|PubMed:4880759}.

Biophysicochemical properties: Kinetic parameters: KM=0.81 mM for beta-aspartylleucine (at pH 8.0) {ECO:0000269|PubMed:4880759}; pH dependence: Optimum pH is 7.5. Active over a wide pH range. {ECO:0000269|PubMed:4880759};

Subcellular location: Cytoplasm {ECO:0000269|PubMed:7876157}.

Ptm: Carboxylation allows a single lysine to coordinate two zinc ions (PubMed:12718528, PubMed:12946361, PubMed:15882050, PubMed:16289685). {ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685}.

Disruption phenotype: No observable phenotype. Does not result in reduced stationary phase or heat shock survival. Approximately 31% of the enzyme activity present. {ECO:0000269|PubMed:7876157}.

Similarity: Belongs to the peptidase M38 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu. {ECO:0000269\|PubMed:12718528, ECO:0000269\|PubMed:15882050, ECO:0000269\|PubMed:4880759, ECO:0000269\|PubMed:7876157}.


Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:12718528, ECO:0000269\|PubMed:12946361, ECO:0000269\|PubMed:15882050}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269\|PubMed:12718528, ECO:0000269\|PubMed:12946361, ECO:0000269\|PubMed:15882050}; Note=Binds 2 Zn(2+) ions per subunit. Has highest activity with Zn(2+) ions, but is also active with Co(2+) ions. {ECO:0000269\|PubMed:12718528, ECO:0000269\|PubMed:12946361, ECO:0000269\|PubMed:15882050};
Activity regulation:		P-hydroxymercuribenzoate causes a slight inhibition (8 to 17 %). Iodoacetamide, o-iodosobenzoate and ammonium persulfate do not inhibit the enzyme activity. {ECO:0000269\|PubMed:4880759}.
Biophysicochemical properties:		Kinetic parameters: KM=0.81 mM for beta-aspartylleucine (at pH 8.0) {ECO:0000269\|PubMed:4880759}; pH dependence: Optimum pH is 7.5. Active over a wide pH range. {ECO:0000269\|PubMed:4880759};
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:7876157}.
Ptm:		Carboxylation allows a single lysine to coordinate two zinc ions (PubMed:12718528, PubMed:12946361, PubMed:15882050, PubMed:16289685). {ECO:0000269\|PubMed:12718528, ECO:0000269\|PubMed:12946361, ECO:0000269\|PubMed:15882050, ECO:0000269\|PubMed:16289685}.
Disruption phenotype:		No observable phenotype. Does not result in reduced stationary phase or heat shock survival. Approximately 31% of the enzyme activity present. {ECO:0000269\|PubMed:7876157}.
Similarity:		Belongs to the peptidase M38 family. {ECO:0000305}.