Ribosomal-protein-alanine N-acetyltransferase
| ribosomal-protein-alanine N-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.128 | ||||||||
| CAS number | 113383-52-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a ribosomal-protein-alanine N-acetyltransferase (EC 2.3.1.128) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + ribosomal-protein L-alanine CoA + ribosomal-protein N-acetyl-L-alanine
Thus, the two substrates of this enzyme are acetyl-CoA and ribosomal-protein L-alanine, whereas its two products are CoA and ribosomal-protein N-acetyl-L-alanine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase. This enzyme is also called ribosomal protein S18 acetyltransferase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2CNM, 2CNS, and 2CNT.
References
- Yoshikawa A, Isono S, Sheback A, Isono K (1987). "Cloning and nucleotide sequencing of the genes rimI and rimJ which encode enzymes acetylating ribosomal proteins S18 and S5 of Escherichia coli K12". Mol. Gen. Genet. 209 (3): 481&ndash, 8. doi:10.1007/BF00331153. PMID 2828880.
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