Aminopeptidase

ARTS-1 [1]
Identifiers
Symbol ARTS-1
MEROPS M1

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.[2]

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.[3]

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.[3]

See also

References

  1. ^ a b Protein Data Bank 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. 
  2. ^ Langner, Jürgen; Ansorge, Siegfried (2002). Cellular peptidases in immune functions and diseases 2. Springer. ISBN 0-306-46383-0. 
  3. ^ 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. 

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