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Information on EC 2.3.1.48 - histone acetyltransferase and Organism(s) Rattus norvegicus
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2.3.1.48 histone acetyltransferaseIUBMB Comments
A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
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Word Map
- 2.3.1.48
- rhythm
-
oscillation
-
suprachiasmatic
- chromatin
-
entrain
-
night
- scn
- sleep
- melatonin
- drosophila
-
diurnal
-
pacemaker
-
locomotor
-
light-dark
- nuclei
- deacetylases
-
pineal
-
morning
-
photoperiodic
- retinal
-
draw
- hypothalamus
- hdacs
-
light-induced
- melanogaster
- photoreceptors
-
noise
-
bayesian
-
nocturnal
-
evening
-
daytime
-
deacetylation
-
coherent
-
co-activator
-
oscillatory
- dementia
-
transactivation
- flies
-
neuropeptide
-
wake
-
schedule
-
24-hour
-
pulses
-
circuit
- medicine
-
lengthen
- molecular biology
-
trichostatin
-
mood
-
verbal
-
neuropsychological
- drug development
- tick
- analysis
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
clock, histone acetyltransferase, n-acetyltransferase, tip60, histone acetyltransferases, cbp/p300, creb-binding protein, ep300, crebbp, creb binding protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, histone
-
-
-
-
histone acetokinase
-
-
-
-
histone acetylase
-
-
-
-
histone transacetylase
-
-
-
-
nucleosome-histone acetyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine
ping-pong mechanism, enzyme form NII
-
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine
rapid equilibrium ordered bireactant mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[protein]-L-lysine acetyltransferase
A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].
CAS REGISTRY NUMBER
COMMENTARY
9054-51-7
-
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 + 1,6-hexanediamine
?
-
enzyme form A shows low activity , B not
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
-
?
acetyl-CoA + poly-L-lysine
CoA + N6-acetyllysine
-
enzyme form A, not enzyme form B1 and B2
-
?
acetyl-CoA + 1,5-pentanediamine
?
-
enzyme form A and B, low activity
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A, not enzyme form B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f1, enzyme form A
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f2a1, enzyme form B1 and B2
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 poor substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B is specific for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is a poor substrate
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
the enzyme is involved in ethanol-induced acetylation of histone H3 in hepatocytes, potential mechanism for gene expression activation by the enzyme, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9 and Lys14
-
-
?
additional information
?
-
-
diaminodipropylamine and 1,3-propanediamine are no substrates
-
-
?
additional information
?
-
-
the enzyme modulates gene expression in liver nuclei in an epigenetic manner at high blood alcohol levels, no alteratins of MAP kinase levels, overview
-
-
?
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
additional information
?
-
-
the enzyme modulates gene expression in liver nuclei in an epigenetic manner at high blood alcohol levels, no alteratins of MAP kinase levels, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
the enzyme is involved in ethanol-induced acetylation of histone H3 in hepatocytes, potential mechanism for gene expression activation by the enzyme, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
Mg2+ or Ca2+ required at low concentration of 5 mM, inhibition at 10-20 mM
garcinol
-
both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300
Mg2+
-
Mg2+ or Ca2+ required at low concentration, 5 mM, inhibition at 10-20 mM
p-chloromercuribenzoate
-
strongly inhibits activity of enzyme form B, formation of acyl-enzyme complex
spermidine
-
inhibits histone acetylation at high concentrations, enzyme forms A and B
additional information
-
both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300
-
DNA
-
in vitro, enzyme form A inhibited, enzyme form B relatively insensitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
ethanol induces the enzyme expression in the liver and activates the enzyme at specific lysine residues, e.g. Lys9 or Lys14, mechanisms of ethanol-induced histone H3 acetylation, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 enzyme forms NI and NII from nucleus and 2 enzyme forms CI and CII from cytoplasm
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). NCOA3_RAT
1082
0
115134
Swiss-Prot
Mitochondrion (Reliability: 4)
NAA60_RAT
242
0
27493
Swiss-Prot
other Location (Reliability: 2)
CBP_RAT
2442
0
265424
Swiss-Prot
other Location (Reliability: 2)
CLOCK_RAT
862
0
97004
Swiss-Prot
other Location (Reliability: 2)
KAT5_RAT
513
0
58598
Swiss-Prot
other Location (Reliability: 1)
KAT6A_RAT
1998
0
223331
Swiss-Prot
other Location (Reliability: 2)
KAT7_RAT
612
0
70514
Swiss-Prot
other Location (Reliability: 2)
KAT8_RAT
458
0
52632
Swiss-Prot
other Location (Reliability: 2)
HAT1_RAT
419
0
49241
Swiss-Prot
other Location (Reliability: 1)
NT8F3_RAT
228
2
26038
Swiss-Prot
Secretory Pathway (Reliability: 5)
TF2B_RAT
316
0
34819
Swiss-Prot
other Location (Reliability: 3)
A0A0G2KA75_RAT
487
0
55518
TrEMBL
other Location (Reliability: 2)
A0A8I6GLG6_RAT
581
0
66888
TrEMBL
other Location (Reliability: 3)
A0A8I5ZRH6_RAT
2406
0
261278
TrEMBL
other Location (Reliability: 2)
A0A0A0MY12_RAT
1719
0
193593
TrEMBL
other Location (Reliability: 2)
A0A0G2JWZ8_RAT
281
0
31082
TrEMBL
other Location (Reliability: 2)
A0A0H2UHR5_RAT
459
0
53364
TrEMBL
other Location (Reliability: 4)
A0A8I6A7V0_RAT
258
0
29073
TrEMBL
other Location (Reliability: 2)
M0R4T9_RAT
1857
0
206049
TrEMBL
other Location (Reliability: 2)
A0A8I5ZWI6_RAT
401
0
47289
TrEMBL
Mitochondrion (Reliability: 2)
A0A8I6GLZ3_RAT
2039
0
225904
TrEMBL
other Location (Reliability: 2)
A0A8I6A718_RAT
136
0
15139
TrEMBL
other Location (Reliability: 2)
A0A0G2K9F0_RAT
579
0
66571
TrEMBL
other Location (Reliability: 1)
A0A8I5YBK1_RAT
419
0
49251
TrEMBL
other Location (Reliability: 1)
F1M9G7_RAT
2444
0
265636
TrEMBL
other Location (Reliability: 2)
Q5RJS0_RAT
197
0
21110
TrEMBL
other Location (Reliability: 4)
A0A8I6AGI2_RAT
611
0
70583
TrEMBL
other Location (Reliability: 3)
Q812C1_RAT
44
0
5255
TrEMBL
other Location (Reliability: 5)
A0A8I6AJG3_RAT
546
0
61786
TrEMBL
other Location (Reliability: 3)
A0A8I6AXE6_RAT
297
0
32771
TrEMBL
other Location (Reliability: 3)
D3ZCG0_RAT
522
0
60251
TrEMBL
other Location (Reliability: 3)
A0A8I6A312_RAT
589
0
67826
TrEMBL
other Location (Reliability: 1)
A0A8J8YC15_RAT
765
0
86330
TrEMBL
other Location (Reliability: 3)
A7BJV7_RAT
606
0
69914
TrEMBL
other Location (Reliability: 1)
Q91XT1_RAT
351
0
35189
TrEMBL
other Location (Reliability: 2)
D4ACX5_RAT
833
0
93722
TrEMBL
other Location (Reliability: 4)
A0A8I6G641_RAT
1945
0
215168
TrEMBL
other Location (Reliability: 2)
Q91XT0_RAT
353
0
36049
TrEMBL
other Location (Reliability: 2)
A0A8I5ZN33_RAT
436
0
51239
TrEMBL
Mitochondrion (Reliability: 2)
A0A0A0MXW7_RAT
310
0
34056
TrEMBL
other Location (Reliability: 2)
Q812C2_RAT
63
0
6170
TrEMBL
other Location (Reliability: 2)
A0A0G2QC09_RAT
365
0
38324
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5ZQ84_RAT
417
0
49041
TrEMBL
other Location (Reliability: 1)
A0A8I6ALR8_RAT
494
0
56280
TrEMBL
other Location (Reliability: 3)
A0A0G2K1C6_RAT
1699
0
189894
TrEMBL
other Location (Reliability: 2)
A0A8I6AG08_RAT
384
0
45292
TrEMBL
other Location (Reliability: 1)
A0A8I5Y222_RAT
813
0
91840
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the dietary compound curcumin inhibits p300 histone acetyltransferase activity and prevents heart failure in rats. Therefore, inhibition of p300 HAT activity by the nontoxic dietary compound curcumin may provide a novel therapeutic strategy for heart failure in humans
medicine
-
histone acetylation is significantly increased in retinas from diabetic rats, and this acetylation is inhibited in diabetics treated with minocycline. Both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300, or activators of histone deacetylase, such as theophylline and resveratrol, and are increased by the histone deacetylase inhibitor, suberolylanilide hydroxamic acid. Hyperglycemia causes acetylation of retinal histones and probably other proteins and the acetylation contributes to the hyperglycemia-induced upregulation of proinflammatory proteins and thereby to the development of diabetic retinopathy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gallwitz, D.; Sures, I.
Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei
Biochim. Biophys. Acta
263
315-328
1972
Rattus norvegicus
Fukushima, M.; Ota, K.; Fujimoto, D.; Horiuchi, K.
Nucleosome-histone acetyltransferase from rat liver chromatin
Biochem. Biophys. Res. Commun.
92
1409-1414
1980
Rattus norvegicus
Libby, P.R.
Rat liver nuclear N-acetyltransferases: separation of two enzymes with both histone and spermidine acetyltransferase activity
Arch. Biochem. Biophys.
203
384-389
1980
Rattus norvegicus
Yukioka, M.; Sasaki, S.; Qi, S.L.; Inoue, A.
Two species of histone acetyltransferase in rat liver nuclei
J. Biol. Chem.
259
8372-8377
1984
Rattus norvegicus
Wiktorowicz, J.E.; Campos, K.L.; Bonner, J.
Substrate and product inhibition initial rate kinetics of histone acetyltransferase
Biochemistry
20
1464-1467
1981
Rattus norvegicus
Wiktorowicz, J.E.; Bonner, J.
Studies on histone acetyltransferase. Partial purification and basic properties
J. Biol. Chem.
257
12893-12900
1982
Rattus norvegicus
Garcea, R.L.; Alberts, B.M.
Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells. Evidence for special factors which modify acetylase action
J. Biol. Chem.
255
11454-11463
1980
Rattus norvegicus
Park, P.H.; Lim, R.W.; Shukla, S.D.
Involvement of histone acetyltransferase (HAT) in ethanol-induced acetylation of histone H3 in hepatocytes: potential mechanism for gene expression
Am. J. Physiol. Gastrointest. Liver Physiol.
289
G1124-G1136
2005
Rattus norvegicus
Bardag-Gorce, F.; French, B.A.; Joyce, M.; Baires, M.; Montgomery, R.O.; Li, J.; French, S.
Histone acetyltransferase p300 modulates gene expression in an epigenetic manner at high blood alcohol levels
Exp. Mol. Pathol.
82
197-202
2007
Rattus norvegicus
Morimoto, T.; Sunagawa, Y.; Kawamura, T.; Takaya, T.; Wada, H.; Nagasawa, A.; Komeda, M.; Fujita, M.; Shimatsu, A.; Kita, T.; Hasegawa, K.
The dietary compound curcumin inhibits p300 histone acetyltransferase activity and prevents heart failure in rats
J. Clin. Invest.
118
868-878
2008
Rattus norvegicus
Kadiyala, C.S.; Zheng, L.; Du, Y.; Yohannes, E.; Kao, H.Y.; Miyagi, M.; Kern, T.S.
Acetylation of retinal histones in diabetes increases inflammatory proteins: effects of minocycline and manipulation of histone acetyltransferase (HAT) and histone deacetylase (HDAC)
J. Biol. Chem.
287
25869-25880
2012
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.3.1.48)
Transporter Classification Database (TCDB): 1.I.1.1.3
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