PROSITE documentation PDOC00613

ArgE / dapE / ACY1 / CPG2 / yscS family signatures




Description

The following enzymes have been shown [1,2,3] to be evolutionary and functionally related:

  • 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 2.3.1.35) while in enterobacteria such as Escherichia coli, it is hydrolyzed by acetylornithine deacetylase (EC 3.5.1.16) (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 3.5.1.18) (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 [4] (EC 3.5.1.14) (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 3.4.17.11) (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 zinc-dependent enzyme.
  • Vacuolar carboxypeptidase S (EC 3.4.17.4) (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 3.4.13.3) (carnosinase) from Lactobacillus (gene pepV) [5], 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.

Note:

These proteins belong to families M20A/M20B in the classification of peptidases [6,E1].

Last update:

December 2004 / Patterns and text revised.

Technical section

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

ARGE_DAPE_CPG2_1, PS00758; ArgE / dapE / ACY1 / CPG2 / yscS family signature 1  (PATTERN)

ARGE_DAPE_CPG2_2, PS00759; ArgE / dapE / ACY1 / CPG2 / yscS family signature 2  (PATTERN)


References

1AuthorsMeinnel T., Schmitt E., Mechulam Y., Blanquet S.
TitleStructural and biochemical characterization of the Escherichia coli argE gene product.
SourceJ. Bacteriol. 174:2323-2331(1992).
PubMed ID1551850

2AuthorsBoyen A., Charlier D., Charlier J., Sakanyan V., Mett I., Glansdorff N.
TitleAcetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related.
SourceGene 116:1-6(1992).
PubMed ID1628835

3AuthorsMiller C.G., Miller J.L., Bagga D.A.
TitleCloning and nucleotide sequence of the anaerobically regulated pepT gene of Salmonella typhimurium.
SourceJ. Bacteriol. 173:3554-3558(1991).
PubMed ID1904438

4AuthorsMitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S.
TitleThe primary structure of porcine aminoacylase 1 deduced from cDNA sequence.
SourceJ. Biochem. 112:737-742(1992).
PubMed ID1284246

5AuthorsVongerichten K.F., Klein J.R., Matern H., Plapp R.
TitleCloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme.
SourceMicrobiology 140:2591-2600(1994).
PubMed ID7528082

6AuthorsRawlings N.D., Barrett A.J.
TitleEvolutionary families of metallopeptidases.
SourceMethods Enzymol. 248:183-228(1995).
PubMed ID7674922

E1Sourcehttp://www.uniprot.org/docs/peptidas



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