The following enzymes have been shown [1,2,3] to be evolutionary and
In the biosynthetic pathway from glutamate to arginine, the removal of an
acetyl group from N2-acetylornithine can be catalyzed via two distinct
enzymatic strategies depending on the organism. In some bacteria and in
fungi, the acetyl group is transferred on glutamate by glutamate
N-acetyltransferase (EC 184.108.40.206) while in enterobacteria such as
Escherichia coli, it is hydrolyzed by acetylornithine deacetylase
(EC 220.127.116.11) (acetylornithinase) (AO) (gene argE). AO is a homodimeric
cobalt-dependent enzyme which displays broad specificity and can also
deacylates substrates such as acetylarginine, acetylhistidine,
acetylglutamate semialdehyde, etc.
Succinyldiaminopimelate desuccinylase (EC 18.104.22.168) (SDAP) (gene dapE) is
the enzyme which catalyzes the fifth step in the biosynthesis of lysine
from aspartate semialdehyde: the hydrolysis of succinyl-diaminopimelate to
diaminopimelate and succinate. SDAP is an enzyme that requires cobalt or
zinc as a cofactor.
Aminoacylase-1  (EC 22.214.171.124) (N-acyl-l-amino-acid amidohydrolase)
(ACY1). ACY1 is a homodimeric zinc-binding mammalian enzyme that catalyzes
the hydrolysis of N-α-acylated amino acids (except for aspartate).
Carboxypeptidase G2 (EC 126.96.36.199) (folate hydrolase G2) (gene cpg2) from
Pseudomonas strain RS-16. This enzyme catalyzes the hydrolysis of reduced
and non-reduced folates to pteroates and glutamate. G2 is a homodimeric
Vacuolar carboxypeptidase S (EC 188.8.131.52) (yscS) from yeast (gene CPS1).
Peptidase T (EC 3.4.11.-) (gene pepT) (tripeptidase) from bacteria. This
enzyme catalyzes a variety of tripeptides containing N-terminal methionine,
leucine, or phenylalanine.
Xaa-His dipeptidase (EC 184.108.40.206) (carnosinase) from Lactobacillus (gene
pepV) , a metalloenzyme with activity against β-alanyl-dipeptides
including carnosine (β-alanyl-histidine).
These enzymes share a few characteristics. They hydrolyse peptidic bonds in
substrates that share a common structure, they are dependent on cobalt or zinc
for their activity and they are proteins of 40 Kd to 60 Kd with a number of
regions of sequence similarity.
As signature patterns for these proteins, we selected two of the conserved
regions. The first pattern contains a conserved histidine which could be
involved in binding metal ions and the second pattern contains a number of
conserved charged residues.
These proteins belong to families M20A/M20B in the classification of
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
Meinnel T., Schmitt E., Mechulam Y., Blanquet S.
Structural and biochemical characterization of the Escherichia coli argE gene product.
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