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Literature summary for 2.3.1.256 extracted from

  • Ochaya, S.; Franzen, O.; Buhwa, D.A.; Foyn, H.; Butler, C.E.; Stove, S.I.; Tyler, K.M.; Arnesen, T.; Matovu, E.; Aslund, L.; Andersson, B.
    Characterization of evolutionarily conserved Trypanosoma cruzi NatC and NatA-N-terminal acetyltransferase complexes (2019), J. Parasitol. Res., 2019, 6594212 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
genes encoding TcNaa30, TcNaa35, and TcNaa38, DNA and amino acid sequence determination, comparison, and analysis, recombinant expression of GST-tagged subunits Trypanosoma cruzi

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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Trypanosoma cruzi 5737
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additional information TcNatC and TcNatA proteins physically interact with each other and it is plausible that this interaction takes place in the cytoplasm as suggested by their possible ribosomal cosedimentation. Subcellular localization of subunits, overview Trypanosoma cruzi
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Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi Q4CRN8 AND Q4DLD9 AND Q4D159 Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 subunit, and non-Esmeraldo-like auxiliary Naa38 subunit
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Trypanosoma cruzi Q4DGZ6 AND Q4DJ45 AND Q4D159 non-Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 and Naa38 subunits
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Trypanosoma cruzi CL Brener Q4CRN8 AND Q4DLD9 AND Q4D159 Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 subunit, and non-Esmeraldo-like auxiliary Naa38 subunit
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Trypanosoma cruzi CL Brener Q4DGZ6 AND Q4DJ45 AND Q4D159 non-Esmeraldo-like NatC catalytic Naa30 subunit and auxiliary Naa35 and Naa38 subunits
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Source Tissue

Source Tissue Comment Organism Textmining
amastigote
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Trypanosoma cruzi
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epimastigote
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Trypanosoma cruzi
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additional information the subunits forming the NatC enzyme complex are expressed in the three main life cycle stages of the parasite, form stable complexes in vivo, and partially cosediment with the ribosome in agreement with a cotranslational function. Expression analysis of TcNaa38/TcNaa30 in the parasite Trypanosoma cruzi
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trypomastigote
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Trypanosoma cruzi
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
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Trypanosoma cruzi N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
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ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
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Trypanosoma cruzi CL Brener N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
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ir
additional information analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP Trypanosoma cruzi ?
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additional information analysis of in vitro acetyltransferase activity of GST-tagged TcNaa30: no activity with peptides STPD, EEEIA, MDEL, and MLGP Trypanosoma cruzi CL Brener ?
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Subunits

Subunits Comment Organism
dimer the Trypanosoma cruzi Nat A protein complex consists of an Esmeraldo-like catalytic NatA complex subunit ARD1/TcNaa10 and a non-Esmeraldo-like auxilliary NatA complex subunit Nat1/TcNaa15 Trypanosoma cruzi

Synonyms

Synonyms Comment Organism
NatC
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Trypanosoma cruzi
TcNaa30
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Trypanosoma cruzi
TcNaa35
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Trypanosoma cruzi
TcNatC
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Trypanosoma cruzi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Trypanosoma cruzi

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Trypanosoma cruzi

General Information

General Information Comment Organism
additional information Trypanosoma cruzi NatC protein complex consists of one catalytic subunit TcNaa30 and one predicted auxiliary subunit TcNaa35. TcNatC and TcNatA (EC 2.3.1.255) complex subunits interact in vivo and in vitro Trypanosoma cruzi
physiological function TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species Trypanosoma cruzi