ID:AMPO_HUMAN DESCRIPTION: RecName: Full=Aminopeptidase O; Short=AP-O; EC=3.4.11.-; FUNCTION: Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. COFACTOR: Binds 1 zinc ion per subunit (By similarity). ENZYME REGULATION: Strongly inhibited by ophenanthroline, a metalloprotease inhibitor. Inhibited by arphamenine A, a potent inhibitor of aminopeptidases. Not affected by AEBSF and E-64, which are common inhibitors of serine- and cysteine-proteases, respectively. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 uM for Asn-AMC; SUBCELLULAR LOCATION: Cytoplasm (Potential). TISSUE SPECIFICITY: Predominantly expressed in pancreas, placenta, liver, testis and heart. Expressed at lower level in brain, lung and kidney. SIMILARITY: Belongs to the peptidase M1 family. SEQUENCE CAUTION: Sequence=AAH20194.1; Type=Erroneous initiation; Sequence=BAB55210.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8N6M6
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.