Aminopeptidase

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3QNF.pdb.png
Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1[1]
Identifiers
Pfam PF01433
MEROPS M1
OPM superfamily 256
OPM protein 3mdj

Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein (N-terminus) 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]

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References[edit]

  1. ^ 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. 
  2. ^ a b Taylor, Allen (1993). "Aminopeptidases: structure and function". The FASEB Journal 7 (2): 290–8. PMID 8440407. 
  3. ^ Langner, Jürgen; Ansorge, Siegfried (2002). Cellular peptidases in immune functions and diseases 2. Springer. ISBN 0-306-46383-0. [page needed]

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