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Information on EC 2.3.1.33 - histidine N-acetyltransferase
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2.3.1.33 histidine N-acetyltransferaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Synonyms
acetylhistidine synthetase, acetyltransferase, histidine, HISAT, histidine acetyltransferase, N-acetyltransferase 16, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylhistidine synthetase
-
-
-
-
acetyltransferase, histidine
-
-
-
-
HISAT
histidine acetyltransferase
-
-
-
-
N-acetyltransferase 16
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-histidine N-acetyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9027-59-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 1-methyl-L-histidine
CoA + 1-methyl-N-acetyl-L-histidine
-
23% activity compared to that with L-histidine
-
?
acetyl-CoA + 3-methyl-L-histidine
CoA + 3-methyl-N-acetyl-L-histidine
-
71% activity compared to that with L-histidine
-
?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
-
with D-histidine 12-20% of the activity with L-histidine
-
?
acetyl-CoA + L-histidine
CoA + N-acetyl-L-histidine
-
strictly specific for the substrates
-
?
additional information
?
-
the recombinant human NAT16 protein has only trace enzyme activity for N-acetyl-L-histidine synthesis
-
-
?
additional information
?
-
-
the recombinant human NAT16 protein has only trace enzyme activity for N-acetyl-L-histidine synthesis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by EDTA, Cd2+, Mg2+, Mn2+, Sr2+, Ca2+, Pb2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity during peroids of starvation and feeding in brain and lens
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the amount of enzyme activity is related to starvation and feeding of the fish
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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
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-
the amount of enzyme activity is related to starvation and feeding of the fish
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-
the amount of enzyme activity is related to starvation and feeding of the fish
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
additional information
-
partial amino acid sequences determination and analysis using mass spectrometry and Edman degradation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HISAT_ORENI
337
0
38413
Swiss-Prot
other Location (Reliability: 2)
HISAT_SCOAU
337
0
38228
Swiss-Prot
other Location (Reliability: 3)
HISAT_XENTR
324
0
36276
Swiss-Prot
other Location (Reliability: 2)
A0A6J8APG9_MYTCO
623
0
70321
TrEMBL
other Location (Reliability: 3)
A0A4Y1K9V2_REHGL
281
0
31332
TrEMBL
other Location (Reliability: 2)
A0A6J8C1G4_MYTCO
321
0
36642
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baslow, M.H.
N-Acetyl-L-histidine synthetase activity from the brain of the killifish
Brain Res.
3
210-213
1966
Fundulus heteroclitus
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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
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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
-
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
Oreochromis niloticus (I3J7Q8), Homo sapiens (Q8N8M0), Homo sapiens, Scomber australasicus (U3U715)
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