CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.630 | Aminopeptidase |
|
3.40.630.30 | Gcn5-related N-acetyltransferase (GNAT) |
Domain Context
CATH Clusters
| Superfamily | 3.40.630.30 |
| Functional Family | Glycylpeptide N-tetradecanoyltransferase |
Enzyme Information
| 2.3.1.97 |
Glycylpeptide N-tetradecanoyltransferase.
based on mapping to UniProt P14743
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal- N-tetradecanoylglycyl-[protein].
-!- The enzyme catalyzes the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. -!- It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. -!- The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
|
UniProtKB Entries (1)
| P14743 |
NMT_YEAST
Saccharomyces cerevisiae S288C
Glycylpeptide N-tetradecanoyltransferase
|
PDB Structure
| PDB | 1IIC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis.
Biochemistry
|