Information on EC 2.3.1.B34 - [protein]-L-lysine N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.B34
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RECOMMENDED NAME
GeneOntology No.
[protein]-L-lysine N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [an AMP-forming acyl-CoA synthase]-L-lysine = CoA + [an AMP-forming acyl-CoA synthase]-N6-acetyl-L-lysine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:AMP-forming acyl-CoA synthase acetyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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A0A0J9WZQ9
UniProt
Manually annotated by BRENDA team
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A0A0J9WZQ9
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
show the reaction diagram
acetyl-CoA + [acetyl coenzyme A synthase Mxan_2570]-L-lysine622
CoA + N-acetyl-[acetyl coenzyme A synthase Mxan_2570]-L-lysine622
show the reaction diagram
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
show the reaction diagram
acetyl-CoA + [BtyA]-L-Lys
CoA + [BtyA]-N6-acetyl-L-Lys
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaA]-L-Lys
CoA + [DcaA]-N6-acetyl-L-Lys
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaB]-L-Lys
CoA + [DcaB]-N6-acetyl-L-Lys
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaC]-L-Lys
CoA + [DcaC]-N6-acetyl-L-Lys
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [LcsB mutant L500V]-L-Lys
CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
show the reaction diagram
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wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue
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?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
show the reaction diagram
acetyl-CoA + [PimA]-L-Lys534
CoA + [PimA]-N6-acetyl-L-Lys534
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase
alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation
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?
acetyl-CoA + [VcsA]-L-Lys
CoA + [VcsA]-N6-acetyl-L-Lys
show the reaction diagram
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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?
additional information
?
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enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
show the reaction diagram
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
show the reaction diagram
acetyl-CoA + [BtyA]-L-Lys
CoA + [BtyA]-N6-acetyl-L-Lys
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
-
-
?
acetyl-CoA + [DcaA]-L-Lys
CoA + [DcaA]-N6-acetyl-L-Lys
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
-
-
?
acetyl-CoA + [DcaB]-L-Lys
CoA + [DcaB]-N6-acetyl-L-Lys
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
-
-
?
acetyl-CoA + [DcaC]-L-Lys
CoA + [DcaC]-N6-acetyl-L-Lys
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
-
-
?
acetyl-CoA + [LcsB mutant L500V]-L-Lys
CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
show the reaction diagram
-
wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue
-
-
?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
show the reaction diagram
acetyl-CoA + [PimA]-L-Lys534
CoA + [PimA]-N6-acetyl-L-Lys534
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase
alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation
-
?
acetyl-CoA + [VcsA]-L-Lys
CoA + [VcsA]-N6-acetyl-L-Lys
show the reaction diagram
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
-
-
?
additional information
?
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enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADP+ negatively regulates an acetyltransferase Mxan_3215, at physiologic concentrations. The enzyme possesses an NAD(P)-binding domain fused to the Gcn5-type N-acetyltransferase domain. NADP+ binding has strong effects on enzyme activity. The Gly11 residue of Mxan_3215 plays an important role in NADP+ binding
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
stimulates the activity via conformational changes that occur upon binding to the amino acid-binding-domain
L-cysteine
stimulates the activity via conformational changes that occur upon binding to the amino acid-binding-domain
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056
acetyl-CoA
pH 7.7, 37C
0.0039
[AcsA]-L-Lys
pH 7.7, 37C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049
acetyl-CoA
Saccharopolyspora erythraea
A4FK18
pH 7.7, 37C
0.019
[AcsA]-L-Lys
Saccharopolyspora erythraea
A4FK18
pH 7.7, 37C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86
acetyl-CoA
Saccharopolyspora erythraea
A4FK18
pH 7.7, 37C
29
5.2
[AcsA]-L-Lys
Saccharopolyspora erythraea
A4FK18
pH 7.7, 37C
210557
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G11A
regulation by NADP+ is abolished
G9A
mutation does no affect regulation of activity by NADP+