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Information on EC 2.3.1.254 - N-terminal methionine Nalpha-acetyltransferase NatB
for references in articles please use BRENDA:EC2.3.1.254
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.254 N-terminal methionine Nalpha-acetyltransferase NatB
IUBMB Comments
N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
The enzyme appears in viruses and cellular organisms
- 2.3.1.254
-
auxiliary
- tropomyosins
-
cable
-
nalpha-terminal
-
unacetylated
- met-asp
-
anti-fcepsilonri
Reaction Schemes
show+
=
+
+
an N-terminal L-methionyl-L-asparaginyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein]
+
+
=
+
+
an N-terminal L-methionyl-L-glutaminyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein]
+
+
=
+
+
an N-terminal L-methionyl-L-aspartyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein]
+
+
=
+
+
an N-terminal L-methionyl-L-glutamyl-[protein]
=
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein]
+
Synonyms
naa20, mdm20, nat3p, cra-1, naa25, mdm20p, naa50p, n-acetyltransferase 3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.3.1.88
-
-
formerly, part transferred
-
MDM20
Mdm20p
N-terminal acetyltransferase
N-terminal acetyltransferase B complex catalytic subunit NAA20
NAA20
NAA25
NAT3
Nat3p
natB
NAA20
-
-
-
-
NAA25
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA
(1)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
(3)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
(2)
-
-
-
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
(4)
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
Ac/N-end rule pathway, Arg/N-end rule pathway (eukaryotic)
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nalpha-acetyltransferase
N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA
Q14CX7; P61599
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutamoyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamoyl-[protein] + CoA
Q14CX7; P61599
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
acetyl-CoA + MFGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MFGPEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MIGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MIGPEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLALISRRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLALISRRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLDPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLDPEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGPEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLGTEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLGTGPARWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTGPARWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLLPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl- MLLPEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + MLRPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLRPEEGGRWGRPVGRRRRRPVRVYP
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
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]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q14CX7; P61599
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q14CX7; P61599
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
P61600; Q8BWZ3
Substrates: heterologous expression of human Bax in mouse embryonic fibroblasts (MEFs). Recombinant human Bax is N-terminally (Nt-)acetylated by Naa20 and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of MEF cells. Human Bax displays the N-terminal Met-Asp amino-acid sequence
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
P61600; Q8BWZ3
Substrates: heterologous expression of human Bax in mouse embryonic fibroblasts (MEFs). Recombinant human Bax is N-terminally (Nt-)acetylated by Naa20 and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of MEF cells. Human Bax displays the N-terminal Met-Asp amino-acid sequence
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
Q06504; Q12387
Substrates: heterologous expression of human Bax in Saccharomyces cerevisiae. Recombinant human Bax is N-terminal (Nt-)acetylated by yNaa20p and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. Human Bax displays the N-terminal Met-Asp amino-acid sequence
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[Bax]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[Bax] + CoA
Q06504; Q12387
Substrates: heterologous expression of human Bax in Saccharomyces cerevisiae. Recombinant human Bax is N-terminal (Nt-)acetylated by yNaa20p and that Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. Human Bax displays the N-terminal Met-Asp amino-acid sequence
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Q5AAR6; Q5AB99
Substrates: substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
Products: -
Products: -
?
additional information
?
-
Q5AAR6; Q5AB99
Substrates: substrate specificity of NatB is determined by the first two amino acids of the substrate protein/peptide. The substrate's N-terminus is anchored into the NatB catalytic pocket by hydrogen bonds. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position. No activity with the NatC substrate MLRFVTANSQDNGRPVGRK and with the NatA substrate SASEAG
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme preferably acetylates oligopeptides with N-termini Met-Leu-Xxx-Pro. Furthermore, the enzyme autoacetylates lysines 34, 37, and 140 in vitro
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also shows lysine Nepsilon-acetyltransferase activity with histone 4
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with MKEEVKGRWGRPVGRRRRRPVRVYP and MDELFPLRWGRPVGRRRRRPVRVYP
Products: -
Products: -
?
additional information
?
-
P61599; Q14CX7
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Q06504; Q12387
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Q06504; Q12387
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[influenza virus PA-X]
N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[influenza virus PA-X] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
additional information
?
-
P61599; Q14CX7
Substrates: 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
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-asparginyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q5AAR6; Q5AB99
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61599; Q14CX7
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
P61600; Q8BWZ3
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein]
an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Q06504; Q12387
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Naa20, the catalytic subunit of NatB complex, contributes to hepatocellular carcinoma by regulating the LKB1-AMPK-mTOR axis.
Carcinoma, Hepatocellular
Naa20, the catalytic subunit of NatB complex, contributes to hepatocellular carcinoma by regulating the LKB1-AMPK-mTOR axis.
Influenza, Human
N-Terminal Acetylation by NatB Is Required for the Shutoff Activity of Influenza A Virus PA-X.
Intellectual Disability
Missense NAA20 variants impairing the NatB protein N-terminal acetyltransferase cause autosomal recessive developmental delay, intellectual disability, and microcephaly.
Ischemic Stroke
The relationship between the prognosis of children with acute arterial stroke and polymorphisms of CDKN2B, HDAC9, NINJ2, NAA25 genes.
Microcephaly
Missense NAA20 variants impairing the NatB protein N-terminal acetyltransferase cause autosomal recessive developmental delay, intellectual disability, and microcephaly.
Neoplasms
Naa20, the catalytic subunit of NatB complex, contributes to hepatocellular carcinoma by regulating the LKB1-AMPK-mTOR axis.
Stroke
The relationship between the prognosis of children with acute arterial stroke and polymorphisms of CDKN2B, HDAC9, NINJ2, NAA25 genes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunits Naa20 and Naa25 of enzyme complex NatB
Q5AAR6; Q5AB99
UniProt
brenda
subunits Naa20 and Naa25 of enzyme complex NatB
Q5AAR6; Q5AB99
UniProt
brenda
Q14CX7 i.e. auxiliary subunit NAA25, P61599 i.e. acetyltransferase subunit NAA20
Q14CX7; P61599
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
the enzyme controls the levels of acetyl-coenzyme A by antagonizing the acetyl-CoA hydrolase ACER-1
physiological function
additional information
evolution
P61599; Q14CX7
Nat3p and Mdm20p subunits form a heterodimer, named NatB, which is a member of the NAT family
evolution
Q06504; Q12387
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
evolution
Q5AAR6; Q5AB99
the family of N-terminal acetyltransferases (NATs) has six subtypes with their unique substrate specificity, NatA-NatF. The substrate specificity of Nats is determined by the first two amino acids of the substrate protein/peptide. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position
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
-
evolution
-
the family of N-terminal acetyltransferases (NATs) has six subtypes with their unique substrate specificity, NatA-NatF. The substrate specificity of Nats is determined by the first two amino acids of the substrate protein/peptide. NatB has a unique substrate specificity different from all other NATs, which requires acidic amino acids or their amides at the second position
-
malfunction
-
enzyme knockdown disrupts normal cell-cycle progression and induces cell growth inhibition. Enzyme knockdown results in an increase in G0/G1-phase cells
malfunction
P61599; Q14CX7
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
malfunction
Q06504; Q12387
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
malfunction
Q06504; Q12387
recombinant Bax accumulates in the mitochondria of yeast naa20DELTA (W303 naa20DELTA), but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
malfunction
P61600; Q8BWZ3
Naa25 inactivation is embryonic lethal in homozygocity. Recombinant Bax accumulates in the mitochondria of Naa25-/- MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
malfunction
Q14CX7; P61599
inhibition of MetAP2 expression blocks NatB enzymatic complex formation by retaining the initial methionine of subunit NAA20
malfunction
Q14CX7; P61599
variants Met54Val and Ala80Val of subunit NAA20 have been identified with individuals presenting with developmental delay, intellectual disability, and microcephaly. Both M54V and A80V are impaired in their capacity to form a NatB complex with NAA25, and show reduced catalytic activities toward different NatB substrates
malfunction
-
Naa25 inactivation is embryonic lethal in homozygocity. Recombinant Bax accumulates in the mitochondria of Naa25-/- MEF cells, but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
-
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
-
malfunction
-
recombinant Bax accumulates in the mitochondria of yeast naa20DELTA (W303 naa20DELTA), but does not promote cytochrome c release, suggesting that an additional step is required for full activation of Bax
-
physiological function
-
the enzyme is required for normal levels of global histone acetylation in the germline
physiological function
-
the enzyme is involved in vacuolar protein sorting and cell wall maintenance
physiological function
-
the enzyme Naa50p is important for chromosome segregation
physiological function
-
the NatB complex activity is required for flowering time regulation and for leaf, inflorescence, flower, fruit and embryonic development. NatB-mediated N-alpha-terminal acetylation of proteins is pleiotropically required for Arabidopsis development
physiological function
P61599; Q14CX7
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
physiological function
Q06504; Q12387
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
physiological function
Q06504; Q12387
recombinant human Bax expressed in strain BY4743 is N-terminally (Nt-)acetylated by yNaa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
physiological function
P61600; Q8BWZ3
recombinant human Bax expressed in MEF cells is N-terminal (Nt-)acetylated by Naa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of the cells. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
physiological function
-
recombinant human Bax expressed in MEF cells is N-terminal (Nt-)acetylated by Naa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of the cells. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
-
physiological function
-
the enzyme is involved in vacuolar protein sorting and cell wall maintenance
-
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
-
physiological function
-
recombinant human Bax expressed in strain BY4743 is N-terminally (Nt-)acetylated by yNaa20p. Nt-acetylation of Bax is essential to maintain Bax in an inactive conformation in the cytosol of yeast. N-terminal acetylation modulates Bax targeting to mitochondria. Contribution of Bax Nt-acetylation to its regulation
-
additional information
Q06504; Q12387
Nat3p (equivalent to human NAA20) and Mdm20p (equivalent to human NAA25) are the components of enzyme complex NatB
additional information
Q06504; Q12387
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
additional information
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
additional information
P61600; Q8BWZ3
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
additional information
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
additional information
Q5AAR6; Q5AB99
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
additional information
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
-
additional information
-
Nat3p (equivalent to human NAA20) and Mdm20p (equivalent to human NAA25) are the components of enzyme complex NatB
-
additional information
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
-
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. A hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA Unique molecular mechanism of specific N-terminal acetylation acted by NatB, substrate recognition and acetylation of NatB, overview
-
Show AA Sequence and Transmembrane Helices (1700 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
additional information
heterodimer
P61600; Q8BWZ3
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
heterodimer
-
the NatB enzymatic complex is constituted of two subunits, the NAA20 catalytic subunit and the accessory subunit NAA25
-
heterodimer
Q06504; Q12387
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
heterodimer
-
the NatB enzymatic complex is constituted of two subunits, the Naa3p catalytic subunit and the accessory subunit MDM20
-
additional information
Q5AAR6; Q5AB99
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
additional information
-
the auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. Analysis of the structure of mutant NatB/Naa20(residue 1-170) in complex with a peptide substrate MEAHNK-biotin and of the structure of NatB/Naa20(full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID, structure comparisons, overview
-
additional information
Q06504; Q12387
Nat3p (NAA20) and Mdm20p (NAA25) are the components of enzyme complex NatB
additional information
-
Nat3p (NAA20) and Mdm20p (NAA25) are the components of enzyme complex NatB
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified NatB free and complexed with bisubstrate inhibitor, NatB holoenzyme in the presence of CoA and substrate peptides, best crystals are grown in a condition containing 25 mM MES, pH 6.5, 5% PEG 600, 1.5% PEG 1000, 5% glycerol, 4% 1,3-butanediol, and 5 mM DTT, improved using the NatB complex with Naa20 (residue 1-170), best crystallization condition for NatB and the inhibitor complex is 20 mM Tris, pH 7.5, 20 mM NaCl, 2.2% PEG 4000, 5% glycerol, 4% 1,3-butanediol, and 5 mM DTT, 2-4 days at room temperature, X-ray diffraction structure determination and analysis at 2.33-2.75 A resolution
Q5AAR6; Q5AB99
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A77S
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
E25A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F112A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F112H
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F27A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
F27Y
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
G140A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
H74A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
H74A/T76A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
L23A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
T24P
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
T76A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y124F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138A/Y139A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y138F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y139A
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
Y139F
Q5AAR6; Q5AB99
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
E25A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
F27A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
L23A
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
T24P
-
site-directed mutagenesis of the Naa20 subunit, altered reaction kinetics compared to wild-type enzyme
-
A80V
Q14CX7; P61599
variant of subunit NAA20, identified in an individual presenting with developmental delay, intellectual disability, and microcephaly. Variant impairs the capacity to form a NatB complex with NAA25, and shows reduced catalytic activity toward different NatB substrates. Cellular stability is similar to wild-type
M54V
Q14CX7; P61599
variant of subunit NAA20, identified in an individual presenting with developmental delay, intellectual disability, and microcephaly. Variant impairs the capacity to form a NatB complex with NAA25, and shows reduced catalytic activity toward different NatB substrates. Cellular stability is similar to wild-type
additional information
additional information
Q5AAR6; Q5AB99
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
additional information
-
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
additional information
-
generation of a deletion mutant (residues 1-170) of the catalytic subunit Naa20. Structure of mutant NatB/Naa20 (residue 1-170) in complex with a peptide substrate MEAHNK-biotin and structure of NatB/Naa20 (full-length) in complex with a bisubstrate inhibitor CoA-MDSEVAALVID
-
additional information
-
substitution of the residue at position 2 of yeast NAA20 interferes with NatB complex formation. Substitution of the threonine at position 2 with isoleucine aspartate, pheylalanine and proline decreases subunit NAA20's interaction with subunit NAA25, whereas alanine, cysteine and serine replacements behave as the native NAA20 protein
additional information
P61599; Q14CX7
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
additional information
Q14CX7; P61599
deletion of the first five amino acids of subunit NAA20 or fusion of a peptide to its amino terminal end abolishes its interaction with subunit NAA25. Substitution of the second residue of NAA20 with amino acids with small, uncharged side-chains allows NatB enzymatic complex formation. Replacement by residues with large or charged side-chains interferes with its NAA25 interaction
additional information
-
generation of Naa25-/- MEF cells and of NAA25-knockout mice
additional information
-
generation of Naa25-/- MEF cells and of NAA25-knockout mice
-
additional information
Q06504; Q12387
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
additional information
Q06504; Q12387
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
additional information
-
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
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
-
additional information
-
generation yeast naa20DELTA cells, W303 naa20DELTA, from wild-type strain W303-1B
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant NatB complexes from Escherichia coli by affinity chromatography, to homogeneity
Q5AAR6; Q5AB99
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes NAA20 and NAA25, sequence comparisons, functional recombinant coexpression of a full-length auxiliary subunit Naa25 subunit (residues 1-745) with a full-length (residues 1-188) or a deletion mutant (residues 1-170) of the catalytic subunit Naa20 as heterodimeric NatB holoenzymes in Escherichia coli, recombinant expression of His- and/or FLAG-tagged NatB wild-type and mutants enzymes in Escherichia coli
Q5AAR6; Q5AB99
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Starheim, K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug, J.; Lillehaug, J.
Identification of the human Nalpha-acetyltransferase complex B (hNatB): A complex important for cell-cycle progression
Biochem. J.
415
325-331
2008
Homo sapiens
brenda
Evjenth, R.; Hole, K.; Karlsen, O.; Ziegler, M.; Amesen, T.; Lillehaug, J.
Human Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
J. Biol. Chem.
284
31122-31129
2009
Homo sapiens
brenda
Lee, K.E.; Ahn, J.Y.; Kim, J.M.; Hwang, C.S.
Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae
J. Microbiol.
52
842-848
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Gao, J.; Kim, H.M.; Elia, A.E.; Elledge, S.J.; Colaiacovo, M.P.
NatB domain-containing CRA-1 antagonizes hydrolase ACER-1 linking acetyl-CoA metabolism to the initiation of recombination during C. elegans meiosis
PLoS Genet.
11
e1005029
2015
Caenorhabditis elegans
brenda
Ferrandez-Ayela, A.; Micol-Ponce, R.; Sanchez-Garcia, A.; Alonso-Peral, M.; Micol, J.; Ponce, M.
Mutation of an Arabidopsis NatB N-alpha-terminal acetylation complex component causes pleiotropic developmental defects
PLoS ONE
8
e80697
2013
Arabidopsis thaliana
brenda
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
Cell Rep.
24
851-860
2018
Homo sapiens (P61599 AND Q14CX7), Saccharomyces cerevisiae (Q06504 AND Q12387), Saccharomyces cerevisiae ATCC 204508 (Q06504 AND Q12387)
brenda
Alves, S.; Neiri, L.; Rodrigues Chaves, S.; Trindade, V.D.; Manon, S.; Dominguez, V.; Pintado, B.; Jonckheere, V.; Van Damme, P.; Silva, R.D.; Aldabe, R.; Corte-Real, M.
N-terminal acetylation modulates Bax targeting to mitochondria
Int. J. Biochem. Cell Biol.
95
35-42
2018
Mus musculus (P61600 AND Q8BWZ3), Mus musculus, Mus musculus C57BL/6 (P61600 AND Q8BWZ3), Saccharomyces cerevisiae (Q06504 AND Q12387), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q06504 AND Q12387)
brenda
Hong, H.; Cai, Y.; Zhang, S.; Ding, H.; Wang, H.; Han, A.
Molecular basis of substrate specific acetylation by N-terminal acetyltransferase NatB
Structure
25
641-649.e3
2017
Candida albicans (Q5AAR6 AND Q5AB99), Candida albicans, Candida albicans ATCC MYA-2876 (Q5AAR6 AND Q5AB99)
brenda
Morrison, J.; Altuwaijri, N.K.; Brnstad, K.; Aksnes, H.; Alsaif, H.S.; Evans, A.; Hashem, M.; Wheeler, P.G.; Webb, B.D.; Alkuraya, F.S.; Arnesen, T.
Missense NAA20 variants impairing the NatB protein N-terminal acetyltransferase cause autosomal recessive developmental delay, intellectual disability, and microcephaly
Genet. Med.
23
2213-2218
2021
Homo sapiens (Q14CX7 and P61599)
brenda
Lasa, M.; Neri, L.; Carte, B.; Gazquez, C.; Aragon, T.; Aldabe, R.
Maturation of NAA20 aminoterminal end is essential to assemble NatB N-terminal acetyltransferase complex
J. Mol. Biol.
432
5889-5901
2020
Homo sapiens (Q14CX7 and P61599), Drosophila melanogaster
brenda
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