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 |
Enzyme Information
2.3.1.271 |
L-glutamate-5-semialdehyde N-acetyltransferase.
based on mapping to UniProt E9P8D2
Acetyl-CoA + L-glutamate-5-semialdehyde = CoA + N-acetyl-L-glutamate 5-semialdehyde.
-!- The enzyme, characterized from the yeast Saccharomyces cerevisiae Sigma-1278b, N-acetylates L-glutamate-5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. -!- Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. -!- The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
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UniProtKB Entries (1)
E9P8D2 |
MPR1_YEASX
Saccharomyces cerevisiae
N-acetyltransferase MPR1
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PDB Structure
PDB | 3W6X |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism
Proc.Natl.Acad.Sci.USA
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