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Literature summary for 2.3.1.255 extracted from

  • McTiernan, N.; Stoeve, S.I.; Aukrust, I.; Marli, M.T.; Myklebust, L.M.; Houge, G.; Arnesen, T.
    NAA10 dysfunction with normal NatA-complex activity in a girl with non-syndromic ID and a de novo NAA10 p.(V111G) variant - a case report (2018), BMC Med. genet., 19, 47 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.255

Cloned(Commentary)

Cloned (Comment) Organism
gene NAA10, genotyping, recombinant expression of His-MBP-tagged wild-type and mutant Naa10 in Escherichia coli and in HeLa cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
V111G a naturally occuring 332 T > G missense mutant, the mutant Naa10 has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. NAA10-V111G has a reduced stability compared to wild-type NAA10, and in vitro acetylation assays reveal a reduced enzymatic activity of monomeric NAA10-V111G but not for NAA10-V111G in complex with NAA15 (NatA enzymatic activity). A glycine in position 111 instead of valine will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or acetyl-CoA binding Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P41227 AND Q9BXJ9 subunits Naa10 and Naa15 of NatA enzyme complex
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrates are SESS24 or EEEI24. The ability of NAA10-V111G to acetylate the acidic N-termini EEEI24 is highly reduced compared to wild-type enzyme Homo sapiens ?
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Synonyms

Synonyms Comment Organism
NAA10-NAA15
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 Homo sapiens
NAA10-NAA15 protein complex
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 Homo sapiens
NatA
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 Homo sapiens
NatA protein complex
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 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
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 Homo sapiens

General Information

General Information Comment Organism
malfunction NAA10 variants have been found in patients with an X-linked developmental disorder called Ogden syndrome in its most severe form and, in other familial or de novo cases, with variable degrees of syndromic intellectual disability (ID) affecting both sexes. The mutant NAA10-V111G has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. The syndromic cases may also require a degree of compromised NatA function. The Naa10-V111G phenotype shows mild/moderate non-syndromic intellectual disability, and delayed motor and language development, but normal behavior without autistic traits. The blood leukocyte X-inactivation pattern is within normal range (80/20) Homo sapiens
additional information NatA homology modeling. Residue V111 is located towards the end of the beta5 strand, and a valine in this position is highly conserved in NAA10 homologues as well as in several other NAT catalytic subunits for which crystal structures have been solved. The side chain of V111 is forming a hydrophobic pocket together with Y145, M147, L119 and L109. It is also in close proximity to the sulfur group of acetyl-CoA, which seems to indicate a role for V111 in positioning of acetyl-CoA. A glycine in this position will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or AcCoA binding Homo sapiens
physiological function the NAA10-NAA15 (NatA) protein complex is an N-terminal acetyltransferase responsible for acetylating about of eukaryotic proteins Homo sapiens