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Information on EC 2.3.1.57 - diamine N-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A951
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2.3.1.57 diamine N-acetyltransferaseIUBMB Comments
Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
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Word Map
- 2.3.1.57
- polyamine
- ornithine
- s-adenosylmethionine
- n1-acetylspermidine
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denspm
- pao
- n1,n11-diethylnorspermine
- n1,n12-bisethylspermine
- alpha-difluoromethylornithine
- analysis
-
superinduction
- antizyme
- drug development
-
malme-3m
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n1-acetylation
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gcn5-related
- pharmacology
-
bisguanylhydrazone
- medicine
- adometdc
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
spermidine/spermine n1-acetyltransferase, spermidine n1-acetyltransferase, ssat1, ssat2, spermidine acetyltransferase, spermidine/spermine acetyltransferase, spermidine/spermine-n1-acetyltransferase, ssat-1, spermidine n-acetyltransferase, ssatx, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase
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acetyltransferase, putrescine
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diamine acetyltransferase
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N1-SAT
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N1SSAT
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putrescine (diamine)-acetylating enzyme
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putrescine acetylase
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putrescine acetyltransferase
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putrescine N-acetyltransferase
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SAT
spermidine acetyltransferase
spermidine N1-acetyltransferase
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spermidine/spermine N1-acetyltransferase
SSAT
spermidine acetyltransferase
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spermidine/spermine N1-acetyltransferase
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SSAT
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alkane-alpha,omega-diamine N-acetyltransferase
Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
CAS REGISTRY NUMBER
COMMENTARY
54596-36-0
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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
additional information
?
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spermine binding structure by X-ray diffraction scattering analysis, overview
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?
additional information
?
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the enzyme does not acetylate RcsB in vitro
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additional information
?
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the enzyme does not acetylate RcsB in vitro
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme acetylates and thus neutralizes toxic polyamines
physiological function
the enzyme is a modulator of Escherichia coli transcription through its ability to interact with the transcription factor RcsB. The enzyme interacts with the DNA-binding domain of RcsB and this interaction might be responsible for enzyme-dependent inhibition of RcsB-dependent small RNA rprA transcription
physiological function
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a key enzyme that transfers the acetyl group from acetyl-CoA to either the N-1 or N-8 position of spermidine, thereby reducing the intracellular polyamine level
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
X-ray crystallography, the dodecamer is organized as a hexamer of dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.2 M ammonium phosphate monobasic, 0.1 M Tris, 50% (w/v) 2-methyl-2,4-pentanediol, pH 8.5
small angle X-ray scattering curves from two sets of a two-fold dilution series containing five sample dilutions of enzyme with and without presence of spermine
in complex with spermidine and CoA, sitting drop vapor diffusion method, using 0.1 M Ca-acetate, 0.05 M Na-cacodylate pH 6.5, and 9% (w/v) PEG8000
purified recombinant enzyme, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 40 mg/ml protein in 10 mM HEPES-KOH pH 7.5, 50 mM CoA, 50 mM spermidine, 300 mM KCl, 0.1 mM EDTA, 6 mM 2-mercaptoethanol, 10% glycerol, 10 mM PMSF, 0.02% Brij-35, with 0.001 ml of reservoir solution containing 50 mM sodium cacodylate, pH 6.5, 9% w/v PEG 8000, 0.1 M calcium acetate, and equilibration against 0.5 ml reservoir solution, 20°C, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E33Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E55Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E74Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E83Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
O85E
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
Q53A
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
Y133F
the mutant shows increased enzyme activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex S200 gel filtration
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography and concanavalin A affinity chromatography, followed by gel filtration
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Ni-NTA column chromatography and Superdex S200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene speG, recombinant enzyme expression in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niiyama, M.; Sugiyama, S.; Hirose, M.; Ishikawa, S.; Tomitori, H.; Higashi, K.; Yamashita, T.; Adachi, H.; Takano, K.; Murakami, S.; Murata, M.; Inoue, T.; Mori, Y.; Kashiwagi, K.; Matsumura, H.; Igarashi, K.
Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli
Acta Crystallogr. Sect. F
69
884-887
2013
Escherichia coli
Weigand, S.; Filippova, E.V.; Kiryukhina, O.; Anderson, W.F.
Small angle X-ray scattering data and structure factor fitting for the study of the quaternary structure of the spermidine N-acetyltransferase SpeG
Data Brief
6
47-52
2016
Escherichia coli (P0A951)
Filippova, E.V.; Weigand, S.; Kiryukhina, O.; Wolfe, A.J.; Anderson, W.F.
Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli
Acta Crystallogr. Sect. D
75
545-553
2019
Escherichia coli (P0A951), Escherichia coli
Sugiyama, S.; Ishikawa, S.; Tomitori, H.; Niiyama, M.; Hirose, M.; Miyazaki, Y.; Higashi, K.; Murata, M.; Adachi, H.; Takano, K.; Murakami, S.; Inoue, T.; Mori, Y.; Kashiwagi, K.; Igarashi, K.; Matsumura, H.
Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase
Int. J. Biochem. Cell Biol.
76
87-97
2016
Escherichia coli (A0A0M3KKU5), Escherichia coli, Escherichia coli LY180 (A0A0M3KKU5)
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