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Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Aminopeptidases are used in essential cellular functions. Many, but not all, of these peptidases are zinc Metalloenzymes.^[2]

Some aminopeptidases are monomeric, and others are assemblies of relatively high mass (50 kDa) subunits. CDNA sequences are available for several aminopeptidases and a crystal structure of the open state of human endoplasmic reticulum Aminopeptidase 1 ERAP1 is presented here.^[1] Amino acid sequences determined directly or deduced from cDNAs indicate some amino acid sequence homologies in organisms as diverse as Escherichia coli and mammals, particularly in catalytically important residues or in residues involved in metal ion binding.^[2]

One important aminopeptidase is a zinc-dependent enzyme produced and secreted by glands of the small intestine. It helps the enzymatic digestion of proteins. Additional digestive enzymes produced by these glands include dipeptidases, maltase, sucrase, lactase, and enterokinase.^[3]

References

^ ^a ^b PDB 3QNF: Vollmar, M.; Kochan, G.; Krojer, T.; Harvey, D.; Chaikuad, A.; Allerston, C.; Muniz, J.R.C.; Raynor, J. et al. (2011). Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1. doi:10.2210/pdb3qnf/pdb.
^ ^a ^b Taylor, Allen (1993). "Aminopeptidases: structure and function". The FASEB Journal 7 (2): 290–8. PMID 8440407. http://www.fasebj.org/cgi/pmidlookup?view=long&pmid=8440407.
^ Langner, Jürgen; Ansorge, Siegfried (2002). Cellular peptidases in immune functions and diseases 2. Springer. ISBN 0-306-46383-0. ^{[page needed]}

External links

Aminopeptidases at the US National Library of Medicine Medical Subject Headings (MeSH)

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1. 胆汁うっ滞系酵素の測定（アルカリホスファターゼ、5' -ヌクレオチダーゼ、γ-グルタミルトランスペプチダーゼなど） enzymatic measures of cholestasis eg alkaline phosphatase 5 nucleotidase gamma glutamyl transpeptidase
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3. 腸球菌の微生物学 microbiology of enterococci
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English Journal

Enzymes acting on D-amino acid containing peptides.

Asano Y.SourceBiotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, Toyama, Japan. asano@pu-toyama.ac.jp
Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2012;794:397-406.
Using a synthetic oligopeptide (D-Phe)(4), a microorganism Bacillus cereus DF4-B producing alkaline D-peptidase (ADP) was isolated. The enzymatic properties have been characterized; the enzyme showed D-stereospecific dipeptidyl aminopeptidase and endopeptidase activities. The enzyme was active towar
PMID 21956579

Induced and constitutive responses of digestive enzymes to plant toxins in an herbivorous mammal.

Kohl KD, Dearing MD.SourceDepartment of Biology, University of Utah, 257 S. 1400 East, Salt Lake City, UT 84112, USA.
The Journal of experimental biology.J Exp Biol.2011 Dec 15;214(Pt 24):4133-40.
Many plants produce plant secondary compounds (PSCs) that bind and inhibit the digestive enzymes of herbivores, thus limiting digestibility for the herbivore. Herbivorous insects employ several physiological responses to overcome the anti-nutritive effects of PSCs. However, studies in vertebrates ha
PMID 22116755

Japanese Journal

Family M42 aminopeptidase from the syntrophic bacterium Symbiobacterium thermophilum : Characterization using recombinant protein(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Kumaki Yasuko,Ogawa Masahiro,Hirano Takako,Yoshikawa Keiko,Iwasawa Naoya,Yagi Takurou,Hakamata Wataru,Oku Tadatake,Nishio Toshiyuki
Journal of bioscience and bioengineering 111(2), 134-139, 2011-02
The chromosomal DNA of the syntrophic thermophile Symbiobacterium thermophilum contains open reading frames of the genes encoding family M42 aminopeptidases, Pep1079, Pep1080, and Pep1081. To characte …
NAID 110008460324

Biochemical Characterization of Deblocking Aminopeptidases from the Hyperthermophilic Archaeon Thermococcus kodakarensis KOD1

JIA Baolei,LEE Sangmin,PHAM Bang Phuong,KWACK Jae Myeng,JIN Haifeng,LI Jian,WANG Yuhan,CHEONG Gang-Won
Bioscience, Biotechnology, and Biochemistry 75(6), 1160-1166, 2011
… Deblocking aminopeptidase (DAP) is an exoprotease that can release N-terminal amino acids from blocked peptides. … Finally, TkDAP1 was found to have higher deblocking aminopeptidase activity on the substrates of Ac-Leu-pNA and Ac-Ala-Ala-Ala, while TkDAP2 had higher aminopeptidase activity on the substrates of Leu-pNA and Ala-Ala-Ala-pNA. …
NAID 130000723825

「アミノペプチダーゼ」

	Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1
Identifiers
Symbol
Pfam	PF01433
MEROPS	M1
OPM superfamily	256
OPM protein	3mdj
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

　　[★]

英:aminopeptidase
関: ロイシンアミノペプチダーゼ。エキソペプチダーゼ、ペプチダーゼ

N末端からアミノ酸を加水分解する

「dipeptidyl aminopeptidase」

　　[★]

ジペプチジルアミノペプチダーゼ

関: dipeptidyl peptidase

「cytosol aminopeptidase I」

　　[★] シトソールアミノペプチダーゼI

「alanine aminopeptidase」

　　[★] アラニンアミノペプチダーゼ

「alanine-aminopeptidase」