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Aminopeptidase
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== Function == | == Function == | ||
| - | [[Aminopeptidase|Aminopeptidases]] (AP) ([[EC]] 3) are metal - mostly Zn-dependent enzymes involved in the digestion of proteins. '''Cytosol AP''' (Cyt-AP | + | [[Aminopeptidase|Aminopeptidases]] (AP) ([[EC]] 3) are metal - mostly Zn-dependent enzymes involved in the digestion of proteins. '''Cytosol AP''' (Cyt-AP) and '''AP N''' (APN) remove N-terminal amino acids. The AP are classified by the amino acid which they hydrolyze. Other types of AP are:<br /> |
* '''Cold-activated AP''' (Col-AP)<br /> | * '''Cold-activated AP''' (Col-AP)<br /> | ||
* '''Heat stable AP''' from ''Thermus thermophilus'' (AmpT)<br /> | * '''Heat stable AP''' from ''Thermus thermophilus'' (AmpT)<br /> | ||
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* '''Alanine aminopeptidase''' is called '''aminopeptidase N'''. See details in [[Aminopeptidase N]].<br /> | * '''Alanine aminopeptidase''' is called '''aminopeptidase N'''. See details in [[Aminopeptidase N]].<br /> | ||
* '''Aminopeptidase C''' is a Phe aminopeptidase from ''Aspergillus niger''<ref>PMID:12571053</ref>.<br /> | * '''Aminopeptidase C''' is a Phe aminopeptidase from ''Aspergillus niger''<ref>PMID:12571053</ref>.<br /> | ||
| - | * '''Deblocking aminopeptidase''' is an exoprotease aminopeptidase which can release N-terminal amino acids from blocked peptides<ref>PMID:21670507</ref>.<br /> | + | * '''Deblocking aminopeptidase''' (DAP) is an exoprotease aminopeptidase which can release N-terminal amino acids from blocked peptides<ref>PMID:21670507</ref>.<br /> |
* '''Beta-peptidyl AP''' (BapA) cleaves N-terminal β-homoamino acid from peptides of length 2 to 6.<ref>PMID:8440407</ref><br />. | * '''Beta-peptidyl AP''' (BapA) cleaves N-terminal β-homoamino acid from peptides of length 2 to 6.<ref>PMID:8440407</ref><br />. | ||
| + | * '''M1 family AP''' are Zn+2 containing amino peptidases<ref>PMID:25530263</ref><br /> | ||
Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide. | Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide. | ||
Current revision
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Additional Resources
For additional information, see:
Amino Acid Synthesis & Metabolism
Streptomyces griseus Aminopeptidase (SGAP)
References
- ↑ Basten DE, Dekker PJ, Schaap PJ. Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase. Appl Environ Microbiol. 2003 Feb;69(2):1246-50. PMID:12571053 doi:10.1128/AEM.69.2.1246-1250.2003
- ↑ Jia B, Lee S, Pham BP, Kwack JM, Jin H, Li J, Wang Y, Cheong GW. Biochemical characterization of deblocking aminopeptidases from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1. Biosci Biotechnol Biochem. 2011;75(6):1160-6. PMID:21670507 doi:10.1271/bbb.110114
- ↑ Taylor A. Aminopeptidases: structure and function. FASEB J. 1993 Feb 1;7(2):290-8. PMID:8440407
- ↑ Cadel S, Darmon C, Pernier J, Hervé G, Foulon T. The M1 family of vertebrate aminopeptidases: role of evolutionarily conserved tyrosines in the enzymatic mechanism of aminopeptidase B. Biochimie. 2015 Feb;109:67-77. PMID:25530263 doi:10.1016/j.biochi.2014.12.009
- ↑ Hanaya K, Suetsugu M, Saijo S, Yamato I, Aoki S. Potent inhibition of dinuclear zinc(II) peptidase, an aminopeptidase from Aeromonas proteolytica, by 8-quinolinol derivatives: inhibitor design based on Zn(2+) fluorophores, kinetic, and X-ray crystallographic study. J Biol Inorg Chem. 2012 Feb 5. PMID:22311113 doi:10.1007/s00775-012-0873-4
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