| EC |
3.5.1.121 |
| Accepted name: |
protein N-terminal asparagine amidohydrolase |
| Reaction: |
N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3 |
| Other name(s): |
NTAN1 (gene name) |
| Systematic name: |
protein N-terminal asparagine amidohydrolase |
| Comments: |
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Stewart, A.E., Arfin, S.M. and Bradshaw, R.A. Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme. J. Biol. Chem. 269 (1994) 23509–23517. [PMID: 8089117] |
| 2. |
Grigoryev, S., Stewart, A.E., Kwon, Y.T., Arfin, S.M., Bradshaw, R.A., Jenkins, N.A., Copeland, N.G. and Varshavsky, A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271 (1996) 28521–28532. [DOI] [PMID: 8910481] |
| 3. |
Cantor, J.R., Stone, E.M. and Georgiou, G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry 50 (2011) 3025–3033. [DOI] [PMID: 21375249] |
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| [EC 3.5.1.121 created 2016] |
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