UniProt ID: B8JLQ9 |
FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. {ECO:0000269|PubMed:21921028}. COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; ACTIVITY REGULATION: Strongly inhibited by potato carboxypeptidase inhibitor, and the chelating agents EDTA and 1,10-phenanthroline. Also inhibited by compounds with multiple carboxylic acid groups such as citrate and succinate, and to a lesser exent the amino acids aspartate and glutamate. Not significantly inhibited by benzylsuccinic acid. {ECO:0000269|PubMed:21921028}. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=346 uM for 3-(2-furyl)acryloyl-Glu-Glu (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=324 uM for 3-(2-furyl)acryloyl-Phe-Phe (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=794 uM for 3-(2-furyl)acryloyl-Phe-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; KM=743 uM for 3-(2-furyl)acryloyl-Lys-Ala (at pH 7.5) {ECO:0000269|PubMed:21921028}; pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:21921028}; SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8IVL8}. TISSUE SPECIFICITY: Expressed in intestinal epithelium. {ECO:0000269|PubMed:21921028}. DEVELOPMENTAL STAGE: Detected in intestine from 3 days post- fertilization onwards. {ECO:0000269|PubMed:21921028}. PTM: N-glycosylated. {ECO:0000269|PubMed:21921028}. SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}. |
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