Information on EC 3.5.1.121 - protein N-terminal asparagine amidohydrolase

for references in articles please use BRENDA:EC3.5.1.121
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EC Tree
IUBMB 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.
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Word Map
  • 3.5.1.121
  • deamidation
  • asparagine-specific
  • e3alpha
  • outwardly
  • r2r3-myb
  • lashley
  • glutamine-specific
The enzyme appears in viruses and cellular organisms
Reaction Schemes
N-terminal L-asparaginyl-[protein]
+
=
N-terminal L-aspartyl-[protein]
+
Synonyms
amidohydrolase for N-terminal asparagine, N-terminal amidase, N-terminal asparagine amidohydrolase, Nt-amidase, NTA1, NTAN1, NTAN1 amidase, NTAN1p amidase, NtN-amidase, PNAD, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3
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PATHWAY SOURCE
PATHWAYS
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