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Literature summary for 2.3.1.254 extracted from

  • Oishi, K.; Yamayoshi, S.; Kozuka-Hata, H.; Oyama, M.; Kawaoka, Y.
    N-terminal acetylation by NatB is required for the shutoff activity of influenza A virus PA-X (2018), Cell Rep., 24, 851-860 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.254

Protein Variants

Protein Variants Comment Organism
additional information construction of NAA20-KO or NAA25-KO cells. Wild-type, NAA20-KO, or NAA25-KO cells are transfected with plasmids encoding PB2, PB1, PA, and NP, with a plasmid for the expression of viral RNA encoding the firefly luciferase, and with a plasmid encoding Renilla luciferase as a transfection control Homo sapiens
additional information the wild-type yeast strain BY4743 transformed with the plasmid encoding wild-type influenza A PA-X, PA-X E2D, or PA-X E2N proteins barely formed any colonies, whereas wild-type yeast transformed with the plasmid encoding PA-X E2A or PA-X E2P viral proteins formed many colonies Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] Homo sapiens
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] Saccharomyces cerevisiae
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] Saccharomyces cerevisiae ATCC 204508
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] Homo sapiens
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] Saccharomyces cerevisiae
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] Saccharomyces cerevisiae ATCC 204508
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] Homo sapiens
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] Saccharomyces cerevisiae
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] Saccharomyces cerevisiae ATCC 204508
-
 an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X] Homo sapiens
-
 N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
-
 ?
additional information Homo sapiens the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals ?
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P61599 AND Q14CX7 subunits Naa20 and Naa25 of enzyme complex NatB
-
Saccharomyces cerevisiae Q06504 AND Q12387 subunits Nat3p and Mdm20p of enzyme complex NatB
-
Saccharomyces cerevisiae ATCC 204508 Q06504 AND Q12387 subunits Nat3p and Mdm20p of enzyme complex NatB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
-
 Homo sapiens an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
-
 Saccharomyces cerevisiae an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
-
 Saccharomyces cerevisiae ATCC 204508 an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
-
 Homo sapiens an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
-
 Saccharomyces cerevisiae an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
-
 Saccharomyces cerevisiae ATCC 204508 an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
-
 Homo sapiens an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
-
 Saccharomyces cerevisiae an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
-
 Saccharomyces cerevisiae ATCC 204508 an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
 ?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
-
 Homo sapiens N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
-
 ?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X] the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. PA-X starts with Met-Glu. Preparation of a series of plasmids encoding PA-X mutants, which possess a NatB-permissive substitution at the second amino acid of E to D (PA-X E2D), to N (PA-X E2N), or to A (PA-X E2A), which is recognized by NatA, but not NatB, or to P (PA-X E2P) Homo sapiens N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
-
 ?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
-
 Saccharomyces cerevisiae an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
-
 ?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
-
 Saccharomyces cerevisiae ATCC 204508 an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
-
 ?
additional information the enzyme NatB acetylates the N-terminal amino acid of polymerase acidic proteins, especially PA-X, of influenza A virus. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals Homo sapiens ?
-
-
additional information NatB catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins and prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn Saccharomyces cerevisiae ?
-
-
additional information NatB catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins and prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn Saccharomyces cerevisiae ATCC 204508 ?
-
-

Subunits

Subunits Comment Organism
More Naa20 and Naa25 are the components of enzyme complex NatB Homo sapiens
More Nat3p (NAA20) and Mdm20p (NAA25) are the components of enzyme complex NatB Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
MDM20
-
 Saccharomyces cerevisiae
Mdm20p
-
 Saccharomyces cerevisiae
N-terminal acetyltransferase B complex catalytic subunit NAA20 UniProt Homo sapiens
NAA20
-
 Homo sapiens
NAA25
-
 Homo sapiens
NAT3
-
 Saccharomyces cerevisiae
Nat3p
-
 Saccharomyces cerevisiae
natB
-
 Homo sapiens
natB
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Homo sapiens
acetyl-CoA
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family Homo sapiens
evolution Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family. Each NAT family member preferentially catalyzes the N-terminal acetylation of the N-terminal amino acid of its target proteins. NatB prefers to acetylate proteins beginning with Met-Asp, Met-Glu, and Met-Asn in yeast and mammals Saccharomyces cerevisiae
malfunction shutoff activity of influenza A viral PA-X is suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB show reduced shutoff activities. Polymerase acidic proteins (PAs) that are not acetylated by NatB lost their function in the viral polymerase complex Homo sapiens
malfunction shutoff activity of influenza A viral PA-X is suppressed in NatB-deficient cells, and PA-X mutants that are not acetylated by NatB show reduced shutoff activities. Polymerase acidic proteins (PAs) that are not acetylated by NatB lost their function in the viral polymerase complex Saccharomyces cerevisiae
additional information Naa20 and Naa25 are the components of enzyme complex NatB Homo sapiens
additional information Nat3p (equivalent to human NAA20) and Mdm20p (equivalent to human NAA25) are the components of enzyme complex NatB Saccharomyces cerevisiae
physiological function N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. N-terminal acetylation modulates diverse protein functions. The N-terminal acetylation by NatB, which comprises the subunits NAA20 and NAA25, is involved in the shutoff activity of influenza virus PA-X. PA-X must be N-terminally acetylated by NatB for its shutoff activity. PA-X cleaves host mRNAs via its endonuclease activity to suppress host protein expression Homo sapiens
physiological function N-terminal acetylation is a major posttranslational modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), NatA through NatF. N-terminal acetylation modulates diverse protein functions. The N-terminal acetylation by NatB, which comprises the subunits Naa3 and MDM20 is essential in the shutoff activity of influenza virus PA-X. PA-X must be N-terminally acetylated by NatB for its shutoff activity. The second amino acid, recognized by NatB, is required for the shutoff activity of PA-X in a NatB-dependent manner. Saccharomyces cerevisiae is used as a model organism Saccharomyces cerevisiae