 |
|
| 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:
References
| 1 | Authors | Meinnel T., Schmitt E., Mechulam Y., Blanquet S. |
| Title | Structural and biochemical characterization of the Escherichia coli argE gene product. | |
| Source | J. Bacteriol. 174:2323-2331(1992). | |
| PubMed ID | 1551850 |
| 2 | Authors | Boyen A., Charlier D., Charlier J., Sakanyan V., Mett I., Glansdorff N. |
| Title | Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related. | |
| Source | Gene 116:1-6(1992). | |
| PubMed ID | 1628835 |
| 3 | Authors | Miller C.G., Miller J.L., Bagga D.A. |
| Title | Cloning and nucleotide sequence of the anaerobically regulated pepT gene of Salmonella typhimurium. | |
| Source | J. Bacteriol. 173:3554-3558(1991). | |
| PubMed ID | 1904438 |
| 4 | Authors | Mitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S. |
| Title | The primary structure of porcine aminoacylase 1 deduced from cDNA sequence. | |
| Source | J. Biochem. 112:737-742(1992). | |
| PubMed ID | 1284246 |
| 5 | Authors | Vongerichten K.F., Klein J.R., Matern H., Plapp R. |
| Title | Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme. | |
| Source | Microbiology 140:2591-2600(1994). | |
| PubMed ID | 7528082 |
| 6 | Authors | Rawlings N.D., Barrett A.J. |
| Title | Evolutionary families of metallopeptidases. | |
| Source | Methods Enzymol. 248:183-228(1995). | |
| PubMed ID | 7674922 |
| E1 | Title | https://www.uniprot.org/docs/peptidas |
| Source | ? |
Copyright
PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to Prosite License or see: prosite_license.html.
Miscellaneous
View entry in original PROSITE document format
View entry in raw text format (no links)