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Literature summary for 3.5.1.121 extracted from

  • Kim, M.K.; Oh, S.J.; Lee, B.G.; Song, H.K.
    Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway (2016), Proc. Natl. Acad. Sci. USA, 113, 12438-12443.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.121

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information asparagine-specific enzyme activity with dipeptides Gln-Val and Gln-Gly, Michaelis-Menten kinetics, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-terminal L-asparaginyl-[protein] + H2O Saccharomyces cerevisiae
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P40354
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information dual specificity of yeast Nta1 (yNta1), importance of second-position residues in Asn/Gln-bearing N-terminal degradation signals (N-degrons), also cf. EC 3.5.1.121 Specific hydrogen bonds stabilize interactions between N-degron peptides and hydrophobic peripheral regions of the active site pocket, interactions between Nta1 and N-degron peptides, detailed overview. The enzyme shows asparagine-specific enzyme activity with dipeptides An-Val and Asn-Gly, Michaelis-Menten kinetics Saccharomyces cerevisiae ?
-
 ?
N-terminal L-asparaginyl-[protein] + H2O
-
 Saccharomyces cerevisiae N-terminal L-aspartyl-[protein] + NH3
-
 ?

Subunits

Subunits Comment Organism
monomer in solution, yNta1 is a monomer containing 14 beta-strands, 11 alpha-helices, and three 310-helices. The core region of the enzyme shows antiparallel and parallel mixed beta-sheets surrounded by helices, and these sixstranded beta-sheets face each other Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
N-terminal amidase
-
 Saccharomyces cerevisiae
Nt-amidase
-
 Saccharomyces cerevisiae
NTA1
-
 Saccharomyces cerevisiae
yNta1
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism the first step of the hierarchically organized Arg/N-end rule pathway of protein degradation is deamidation of the N-terminal glutamine and asparagine residues of substrate proteins to glutamate and aspartate, respectively. These reactions are catalyzed by the N-terminal amidase (Nt-amidase) Nta1 in fungi such as Saccharomyces cerevisiae, and by the glutamine-specific Ntaq1 and asparagine-specific Ntan1 Nt-amidases in mammals. Specific deamidation mechanisms in the first step of the N-end rule pathway Saccharomyces cerevisiae