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Information on EC 2.3.1.33 - histidine N-acetyltransferase for references in articles please use BRENDA:EC2.3.1.33
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
acetylhistidine synthetase, acetyltransferase, histidine, HISAT, histidine acetyltransferase, N-acetyltransferase 16,
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acetylhistidine synthetase
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acetyltransferase, histidine
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histidine acetyltransferase
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HISAT
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N-acetyltransferase 16
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acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine
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Acyl group transfer
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acetyl-CoA:L-histidine N-acetyltransferase
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acetyl-CoA + 1-methyl-L-histidine
CoA + 1-methyl-N-acetyl-L-histidine
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23% activity compared to that with L-histidine
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?
acetyl-CoA + 3-methyl-L-histidine
CoA + 3-methyl-N-acetyl-L-histidine
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71% activity compared to that with L-histidine
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
additional information
?
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acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
-
?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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with D-histidine 12-20% of the activity with L-histidine
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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strictly specific for the substrates
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
additional information
?
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the recombinant human NAT16 protein has only trace enzyme activity for N-acetyl-L-histidine synthesis
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additional information
?
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the recombinant human NAT16 protein has only trace enzyme activity for N-acetyl-L-histidine synthesis
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acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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-
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?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
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?
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acetyl-CoA
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additional information
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no divalent metal ions required
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2-mercaptoethanol
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slightly inhibitory
Cu2+
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complete inhibition
hydroxylamine
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slightly inhibitory
N-ethylmorpholine-HCl buffer
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slightly inhibitory
o-phenanthroline
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slightly inhibitory
p-chloromercuribenzoate
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strong inhibition
Tris-HCl buffer
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slightly inhibitory
additional information
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no inhibition by EDTA, Cd2+, Mg2+, Mn2+, Sr2+, Ca2+, Pb2+
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acetyl-CoA
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15fold stimulation
Acetylcholine
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2.5fold stimulation
ATP
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2.6fold stimulation
glycine
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1.9fold stimulation
Sodium acetate
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3.1fold stimulation
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0.027
acetylcoenzyme A
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1692
purified native enzyme, pH 7.8, 37°C
4.3
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partially purified enzyme
additional information
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tissue distribution
additional information
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enzyme activity during peroids of starvation and feeding in brain and lens
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7 - 9.5
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broad optimum, assay at pH 7.8
7.8
assay at
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7 - 7.7
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pH 7.0: 63% of activity maximum, pH 7.7: activity maximum
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37
assay at
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37 - 50
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37°C: optimum, 50°C: less than 10% activity
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killifish
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brenda
gene Nat16
UniProt
brenda
gene hisat, two HISAT splice variant-1 and -2
UniProt
brenda
gene hisat, two HISAT splice variant-1 and -2
UniProt
brenda
Nile tilapia
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-
brenda
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the amount of enzyme activity is related to starvation and feeding of the fish
brenda
additional information
the HISAT gene is expressed as two splice variants containing an identical ORF but differing lengths of 5'-UTR. Both variants are expressed exclusively in the fish brain and lens
brenda
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brenda
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brenda
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brenda
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the amount of enzyme activity is related to starvation and feeding of the fish
brenda
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brenda
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brenda
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the amount of enzyme activity is related to starvation and feeding of the fish
brenda
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brenda
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additional information
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partial amino acid sequences determination and analysis using mass spectrometry and Edman degradation
additional information
partial amino acid sequences determination and analysis using mass spectrometry and Edman degradation
additional information
partial amino acid sequences determination and analysis using mass spectrometry and Edman degradation
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HISAT_ORENI
337
0
38413
Swiss-Prot
HISAT_SCOAU
337
0
38228
Swiss-Prot
HISAT_XENTR
324
0
36276
Swiss-Prot
A0A4Y1K9V2_REHGL
281
0
31332
TrEMBL
NAT16_HUMAN
369
0
40521
Swiss-Prot
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38500
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1 * 38500, SDS-PAGE
39000
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gel filtration
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monomer
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1 * 38500, SDS-PAGE
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37
the purified enzyme HISAT is an unstable enzyme that is rapidly and irreversibly inactivated during preincubation at 37 °C in the absence of acetyl-CoA
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HISAT is an unstable enzyme that is rapidly and irreversibly inactivated during preincubation at 37 °C in the absence of acetyl-CoA
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native enzyme 4453fold from brain by ammonium sulfate fractionation, dye-ligand affinity chromatography, gel filtration, and anion exchange chromatography followed by ultrafiltration
partial
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gene hisat, DNA and amino acid sequence determination and analysis
gene hisat, DNA and amino acid sequence determination and analysis, the HISAT gene is expressed as two splice variants containing an identical ORF but differing lengths of 5'-UTR. Both variants are expressed exclusively in the fish brain and lens, recombinant expression in a cell-free translation system, and recombinant expression of the two HISAT splice variant-1 and -2 in Oreochromis niloticus
gene Nat16, DNA and amino acid sequence determination and analysis, recombinant expression in a cell-free translation system
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Baslow, M.H.
N-Acetyl-L-histidine synthetase activity from the brain of the killifish
Brain Res.
3
210-213
1966
Fundulus heteroclitus
brenda
Yamada, S.; Tanaka, Y.; Furuichi, M.
Partial purification and characterization of histidine acetyltransferase in brain of Nile tilapia (Oreochromis niloticus)
Biochim. Biophys. Acta
1245
239-247
1995
Oreochromis niloticus
brenda
Yamada, S.; Tanaka, Y.; Sameshima, M.; Furuichi, M.
Effects of starvation and feeding on tissue Na-acetylhistidine levels in Nile tilapia Oreochromis niloticus
Comp. Biochem. Physiol. A
109A
277-283
1994
Oreochromis niloticus
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brenda
Yamada, S.; Arikawa, S.
An ectotherm homologue of human predicted gene NAT16 encodes histidine N-acetyltransferase responsible for Nalpha-acetylhistidine synthesis
Biochim. Biophys. Acta
1840
434-442
2014
Homo sapiens, Homo sapiens (Q8N8M0), Oreochromis niloticus (I3J7Q8), Scomber australasicus (U3U715)
brenda
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