Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Deng, S.; Magin, R.; Wei, X.; Pan, B.; Petersson, E.; Marmorstein, R.
    Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex (2019), Structure, 27, 1057-1070.e4 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.258 recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Homo sapiens
2.3.1.258 recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system Saccharomyces cerevisiae
2.3.1.258 recombinant overexpression of N-terminally GST-tagged SpNatA and SpNaa50 in Escherichia coli Schizosaccharomyces pombe

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.258 purified recombinant ScNatA/Naa50 complex, X-ray diffraction structure determination and analysis at 2.7 A resolution Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.258 additional information recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex Schizosaccharomyces pombe
2.3.1.258 additional information recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.258 additional information
-
 additional information binding kinetics of SpNaa50 and SpNatA, Naa50 tightly binds to NatA Schizosaccharomyces pombe
2.3.1.258 additional information
-
 additional information binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA Homo sapiens
2.3.1.258 additional information
-
 additional information binding kinetics of ScNaa50 and ScNatA Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.258 NaCl SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M Schizosaccharomyces pombe

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.258 Homo sapiens Q9GZZ1 AND P41227 AND Q9BXJ9 NatE complex subunits Naa50, Naa10, and Naa15
-
2.3.1.258 Saccharomyces cerevisiae Q08689 AND P07347 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
2.3.1.258 Saccharomyces cerevisiae ATCC 204508 Q08689 AND P07347 AND P12945 NatE complex subunits Naa50, Naa10 (ARD1), and Naa15 (Nat1)
-
2.3.1.258 Schizosaccharomyces pombe
-
-
-
2.3.1.258 Schizosaccharomyces pombe 972
-
-
-
2.3.1.258 Schizosaccharomyces pombe ATCC 24843
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.258 recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration Homo sapiens
2.3.1.258 recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration Saccharomyces cerevisiae
2.3.1.258 recombinant GST-tagged SpNatA and SpNaa50 from Escherichia coli by glutathione affinity chromatography and gel filtration, SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M Schizosaccharomyces pombe

Synonyms

EC Number Synonyms Comment Organism
2.3.1.258 ARD1
-
 Schizosaccharomyces pombe
2.3.1.258 ARD1
-
 Saccharomyces cerevisiae
2.3.1.258 hNaa50
-
 Homo sapiens
2.3.1.258 hNatA
-
 Homo sapiens
2.3.1.258 NAA10
-
 Schizosaccharomyces pombe
2.3.1.258 NAA10
-
 Homo sapiens
2.3.1.258 NAA10
-
 Saccharomyces cerevisiae
2.3.1.258 NAA15
-
 Schizosaccharomyces pombe
2.3.1.258 NAA15
-
 Homo sapiens
2.3.1.258 NAA15
-
 Saccharomyces cerevisiae
2.3.1.258 Naa50
-
 Schizosaccharomyces pombe
2.3.1.258 Naa50
-
 Homo sapiens
2.3.1.258 Naa50
-
 Saccharomyces cerevisiae
2.3.1.258 NAT1
-
 Schizosaccharomyces pombe
2.3.1.258 NAT1
-
 Saccharomyces cerevisiae
2.3.1.258 NatA/Naa50 complex
-
 Schizosaccharomyces pombe
2.3.1.258 NatA/Naa50 complex
-
 Homo sapiens
2.3.1.258 NatA/Naa50 complex
-
 Saccharomyces cerevisiae
2.3.1.258 NatE
-
 Schizosaccharomyces pombe
2.3.1.258 NatE
-
 Homo sapiens
2.3.1.258 NatE
-
 Saccharomyces cerevisiae
2.3.1.258 ScNaa50
-
 Saccharomyces cerevisiae
2.3.1.258 ScNatA
-
 Saccharomyces cerevisiae
2.3.1.258 SpNaa50
-
 Schizosaccharomyces pombe
2.3.1.258 SpNatA
-
 Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
2.3.1.258 evolution the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions Schizosaccharomyces pombe
2.3.1.258 evolution the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions Homo sapiens
2.3.1.258 evolution the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions Saccharomyces cerevisiae
2.3.1.258 malfunction yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association Schizosaccharomyces pombe
2.3.1.258 malfunction yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association Homo sapiens
2.3.1.258 malfunction yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association. Deletion of ScNaa50 shows no phenotype, while Naa50 knockout in higher organisms has been shown to perturb sister chromatid cohesion Saccharomyces cerevisiae
2.3.1.258 additional information the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50 Schizosaccharomyces pombe
2.3.1.258 additional information the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50 Homo sapiens
2.3.1.258 additional information the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA Saccharomyces cerevisiae
2.3.1.258 physiological function NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview Schizosaccharomyces pombe
2.3.1.258 physiological function NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview Homo sapiens
2.3.1.258 physiological function NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview Saccharomyces cerevisiae