Information on EC 2.3.1.254 - N-terminal methionine Nalpha-acetyltransferase NatB

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.254
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RECOMMENDED NAME
GeneOntology No.
N-terminal methionine Nalpha-acetyltransferase NatB
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA
show the reaction diagram
(1)
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acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
show the reaction diagram
(3)
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acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
show the reaction diagram
(2)
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acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nalpha-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
show the reaction diagram
(4)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ac/N-end rule pathway
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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enzyme knockdown disrupts normal cell-cycle progression and induces cell growth inhibition. Enzyme knockdown results in an increase in G0/G1-phase cells
metabolism
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the enzyme controls the levels of acetyl-coenzyme A by antagonizing the acetyl-CoA hydrolase ACER-1
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + MFGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MFGPEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
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-
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-
?
acetyl-CoA + MIGPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MIGPEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
-
-
-
-
?
acetyl-CoA + MLALISRRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLALISRRWGRPVGRRRRRPVRVYP
show the reaction diagram
-
-
-
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?
acetyl-CoA + MLDPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLDPEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
-
-
-
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?
acetyl-CoA + MLGPEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGPEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
-
-
-
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?
acetyl-CoA + MLGTEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
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?
acetyl-CoA + MLGTGPARWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLGTGPARWGRPVGRRRRRPVRVYP
show the reaction diagram
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-
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?
acetyl-CoA + MLLPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl- MLLPEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
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-
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?
acetyl-CoA + MLRPEEGGRWGRPVGRRRRRPVRVYP
CoA + N-acetyl-MLRPEEGGRWGRPVGRRRRRPVRVYP
show the reaction diagram
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
acetyl-CoA
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at pH 8.5 and 37°C
3.734
MFGPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.185
MIGPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.19
MLALISRRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.091
MLDPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.079
MLGPEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.416
MLGTEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.32
MLGTGPARWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.478
MLLPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.46
MLRPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
MIGPEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.11
MLALISRRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.12
MLDPEEGGRWGRPVGRRRRRPVRVYP, MLGPEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.093
MLGTEEGGRWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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0.038
MLGTGPARWGRPVGRRRRRPVRVYP
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at pH 8.5 and 37°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R84A
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the mutant has more than 80% less activity than the wild type enzyme
Y124F
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the mutant has about 90% less activity than the wild type enzyme