PROSITE documentation PDOC00494
Amidases signature


It has been shown [1,2,3] that several enzymes from various prokaryotic and eukaryotic organisms which are involved in the hydrolysis of amides (amidases) are evolutionary related. These enzymes are listed below.

  • Indoleacetamide hydrolase (EC 3.5.1.-), a bacterial plasmid-encoded enzyme that catalyzes the hydrolysis of indole-3-acetamide (IAM) into indole-3- acetate (IAA), the second step in the biosynthesis of auxins from tryptophan.
  • Acetamidase from Emericella nidulans (gene amdS), an enzyme which allows acetamide to be used as a sole carbon or nitrogen source.
  • Amidase (EC from Rhodococcus sp. N-774 and Brevibacterium sp. R312 (gene amdA). This enzyme hydrolyzes propionamides efficiently, and also at a lower efficiency, acetamide, acrylamide and indoleacetamide.
  • Amidase (EC from Pseudomonas chlororaphis.
  • 6-aminohexanoate-cyclic-dimer hydrolase (EC (nylon oligomers degrading enzyme E1) (gene nylA), a bacterial plasmid encoded enzyme which catalyzes the first step in the degradation of 6-aminohexanoic acid cyclic dimer, a by-product of nylon manufacture [4].
  • Glutamyl-tRNA(Gln) amidotransferase subunit A [5].
  • Mammalian fatty acid amide hydrolase (gene FAAH) [6].
  • A putative amidase from yeast (gene AMD2).
  • Mycobacterium tuberculosis putative amidases amiA2, amiB2, amiC and amiD.

All these enzymes contains in their central section a highly conserved region rich in glycine, serine, and alanine residues. We have used this region as a signature pattern.

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

AMIDASES, PS00571; Amidases signature  (PATTERN)


1AuthorsMayaux J.-F. Cerebelaud E. Soubrier F. Faucher D. Petre D.
TitlePurification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase.
SourceJ. Bacteriol. 172:6764-6773(1990).
PubMed ID2254253

2AuthorsHashimoto Y. Nishiyama M. Ikehata O. Horinouchi S. Beppu T.
TitleCloning and characterization of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coli.
SourceBiochim. Biophys. Acta 1088:225-233(1991).
PubMed ID2001397

3AuthorsChang T.-H. Abelson J.
TitleIdentification of a putative amidase gene in yeast Saccharomyces cerevisiae.
SourceNucleic Acids Res. 18:7180-7180(1990).
PubMed ID2263500

4AuthorsTsuchiya K. Fukuyama S. Kanzaki N. Kanagawa K. Negoro S. Okada H.
TitleHigh homology between 6-aminohexanoate-cyclic-dimer hydrolases of Flavobacterium and Pseudomonas strains.
SourceJ. Bacteriol. 171:3187-3191(1989).
PubMed ID2722746

5AuthorsCurnow A.W. Hong K. Yuan R. Kim S. Martins O. Winkler W. Henkin T.M. Soll D.
TitleGlu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation.
SourceProc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
PubMed ID9342321

6AuthorsCravatt B.F. Giang D.K. Mayfield S.P. Boger D.L. Lerner R.A. Gilula N.B.
TitleMolecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides.
SourceNature 384:83-87(1996).
PubMed ID8900284

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