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Literature summary for 2.3.1.255 extracted from
- From molecular understanding to organismal biology of N-terminal acetyltransferases (2019), Structure, 27, 1053-1055 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genes NAA10 and NAA15, recombinant enzyme complex NatA expression in Spodoptera frugiperda SF9 cells via transfection using the baculovirus system | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| holo-NatA complex in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the uncomplexed Naa10p catalytic subunit, X-ray diffraction structure determination and analysis | Schizosaccharomyces pombe |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
| cytosol | - |
Homo sapiens | 5829 | - |
| cytosol | - |
Schizosaccharomyces pombe | 5829 | - |
| ribosome | near to | Saccharomyces cerevisiae | 5840 | - |
| ribosome | near to | Homo sapiens | 5840 | - |
| ribosome | near to | Schizosaccharomyces pombe | 5840 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 100000 | - |
holo-NatA complex | Schizosaccharomyces pombe |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P41227 AND Q9BXJ9 | NatA subunits Naa10 and Naa15 | - |
| Saccharomyces cerevisiae | P07347 AND P12945 | NatA subunits ARD1 and Nat1 | - |
| Saccharomyces cerevisiae ATCC 204508 | P07347 AND P12945 | NatA subunits ARD1 and Nat1 | - |
| Schizosaccharomyces pombe | Q9UTI3 AND O74985 | NatA subunits ARD1 and Nat1 | - |
| Schizosaccharomyces pombe 972 | Q9UTI3 AND O74985 | NatA subunits ARD1 and Nat1 | - |
| Schizosaccharomyces pombe ATCC 24843 | Q9UTI3 AND O74985 | NatA subunits ARD1 and Nat1 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | N-terminal acetylation (NTA) is an irreversible protein modification | Homo sapiens | ? | - |
- |
 |
| additional information | N-terminal acetylation (NTA) is an irreversible protein modification | Schizosaccharomyces pombe | ? | - |
- |
|
| additional information | typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | N-terminal acetylation (NTA) is an irreversible protein modification | Schizosaccharomyces pombe ATCC 24843 | ? | - |
- |
|
| additional information | N-terminal acetylation (NTA) is an irreversible protein modification | Schizosaccharomyces pombe 972 | ? | - |
- |
|
| additional information | typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the NatA enzyme complex is composed of the subunits Naa10 and Naa15 | Saccharomyces cerevisiae |
| More | the NatA enzyme complex is composed of the subunits Naa10 and Naa15 | Homo sapiens |
| More | the NatA enzyme complex is composed of the subunits Naa10 and Naa15 | Schizosaccharomyces pombe |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ARD1 | - |
Saccharomyces cerevisiae |
| ARD1 | - |
Schizosaccharomyces pombe |
| hNaa10 | - |
Homo sapiens |
| hNaa15 | - |
Homo sapiens |
| NAA10 | - |
Saccharomyces cerevisiae |
| NAA10 | - |
Homo sapiens |
| NAA10 | - |
Schizosaccharomyces pombe |
| NAA15 | - |
Saccharomyces cerevisiae |
| NAA15 | - |
Homo sapiens |
| NAA15 | - |
Schizosaccharomyces pombe |
| NAT1 | - |
Saccharomyces cerevisiae |
| NatA | - |
Saccharomyces cerevisiae |
| NatA | - |
Homo sapiens |
| NatA | - |
Schizosaccharomyces pombe |
| SCNaa15 | - |
Saccharomyces cerevisiae |
| ScNatA | - |
Saccharomyces cerevisiae |
| SpNaa10 | - |
Schizosaccharomyces pombe |
| SpNaa15 | - |
Schizosaccharomyces pombe |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Saccharomyces cerevisiae | |
| acetyl-CoA | - |
Homo sapiens | |
| acetyl-CoA | - |
Schizosaccharomyces pombe | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.) | Saccharomyces cerevisiae |
| evolution | there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.) | Homo sapiens |
| evolution | there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.) | Schizosaccharomyces pombe |
| malfunction | mutations in the X-linked gene NAA10 cause Ogden Syndrome (also known as NAA10-related syndrome), which affects numerous aspects of development. Wide-ranging developmental defects are observed in humans with mutations in NAA10 and NAA15 | Saccharomyces cerevisiae |
| metabolism | the enzyme is involved in the co-translational N-terminal protein modification process, overview | Saccharomyces cerevisiae |
| metabolism | the enzyme is involved in the co-translational N-terminal protein modification process, overview | Homo sapiens |
| metabolism | the enzyme is involved in the co-translational N-terminal protein modification process, overview | Schizosaccharomyces pombe |
| additional information | the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures | Homo sapiens |
| additional information | the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures, and ScNaa10 is similarly and completely locked into a cradle by the surrounding Naa15 helices. ScNaa50 has a robust interaction with ScNatA that is maintained even in high salt concentrations (1 M NaCl) | Saccharomyces cerevisiae |
| additional information | the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures. SpNaa50 has a robust interaction with SpNatA that is maintained even in high salt concentrations (1 M NaCl) | Schizosaccharomyces pombe |
| physiological function | N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification | Saccharomyces cerevisiae |
| physiological function | N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification | Schizosaccharomyces pombe |
| physiological function | N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is estimated to affect up to 90% of human proteins and influences their folding, localization, complex formation, and degradation, along with a variety of cellular functions ranging from apoptosis to gene regulation. NTA is an irreversible protein modification | Homo sapiens |
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