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 3.5.1.4) 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 3.5.1.4) from Pseudomonas chlororaphis.
6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) (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].
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.
PROSITE method (with tools and information) covered by this documentation:
References
1
Authors
Mayaux J.-F. Cerebelaud E. Soubrier F. Faucher D. Petre D.
Title
Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase.
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see prosite_license.html.