Information on EC 2.3.1.57 - diamine N-acetyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.57
-
RECOMMENDED NAME
GeneOntology No.
diamine N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
putrescine degradation III
-
-
spermine and spermidine degradation I
-
-
polyamine pathway
-
-
Arginine and proline metabolism
-
-
Metabolic pathways
-
-
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 hide
54596-36-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
female adults
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
CBS 5777
-
-
Manually annotated by BRENDA team
CBS 5777
-
-
Manually annotated by BRENDA team
CBS 6853
-
-
Manually annotated by BRENDA team
female adults
-
-
Manually annotated by BRENDA team
putative
UniProt
Manually annotated by BRENDA team
Trichosporon melibiosaceum
CBS 6087
-
-
Manually annotated by BRENDA team
Trichosporon melibiosaceum CBS 6087
CBS 6087
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
show the reaction diagram
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetyl-spermidine
show the reaction diagram
3 acetyl-CoA + spermidine
CoA + N1,N4,N8-triacetylspermidine
show the reaction diagram
spermidine is preferred over spermine
-
-
?
acetyl-CoA + (S)-2-[(3-aminopropyl)amino]ethylphosphoric acid
CoA + N-acetyl-(S)-2-[(3-aminopropyl)amino]ethylphosphoric acid
show the reaction diagram
-
WR-2721, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + (S)-2-[(3-aminopropyl)amino]propylphosphoric acid
CoA + N-acetyl-(S)-2-[(3-aminopropyl)amino]propylphosphoric acid
show the reaction diagram
-
WR-44923, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
show the reaction diagram
acetyl-CoA + 1,3-diaminopropane
CoA + ?
show the reaction diagram
-
-
-
?
acetyl-CoA + 1,3-diaminopropane
CoA + N1-acetyl-1,3-diaminopropane
show the reaction diagram
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
show the reaction diagram
acetyl-CoA + 1,6-diaminohexane
CoA + N1-acetyl-1,6-diaminohexane
show the reaction diagram
acetyl-CoA + 1,7-diaminoheptane
CoA + N1-acetyl-1,7-diaminoheptane
show the reaction diagram
-
-
-
-
?
acetyl-CoA + 15-deoxyspergualin
?
show the reaction diagram
-
antitumor and immunosuppressive agent 15-deoxyspergualin, about 18% of the rate with spermidine
-
-
?
acetyl-CoA + 2-[(aminopropyl)amino]ethanethiol
CoA + N-acetyl-2-[(aminopropyl)amino]ethanethiol
show the reaction diagram
-
radioprotective drug WR-1065, lower affinity than for spermidine, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + 6,6-difluorospermidine
CoA + N1-acetyl-6,6-difluorospermidine
show the reaction diagram
-
16.6% of the rate with spermidine
-
-
?
acetyl-CoA + 7,7-difluorospermidine
CoA + N1-acetyl-7,7-difluorospermidine
show the reaction diagram
-
19.7% of the rate with spermidine
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
show the reaction diagram
-
reaction occurs in vivo and in vitro, but only in presence of increased enzyme levels, amantadine may be a specific drug substrate for SSAT
-
?
acetyl-CoA + aminopropylcadaverine
?
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-acetylphenylethylamine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
?
acetyl-CoA + diethylenetriamine
CoA + ?
show the reaction diagram
-
-
-
?
acetyl-CoA + diethylenetriamine
CoA + N1-acetyl-diethylenetriamine
show the reaction diagram
-
-
-
?
acetyl-CoA + eIF5A
CoA + acytyl-eIF5A
show the reaction diagram
-
-
selective acetylation of the hypusine and/or deoxyhypusine residue of translation initiation factor eIF5A, resulting in loss of eIF5A activity. Hypusine or deoxyhypusine, as the free amino acid, do not act as a substrate for isoform SSAT1
-
?
acetyl-CoA + ethylenediamine
CoA + N1-acetyl-ethylenediamine
show the reaction diagram
-
-
-
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
show the reaction diagram
acetyl-CoA + histone
CoA + N-acetylhistone
show the reaction diagram
-
-
-
-
?
acetyl-CoA + N-(n-butyl)-1,3-diaminopropane
CoA + N1-acetyl-N3-(n-butyl)-1,3-diaminopropane
show the reaction diagram
-
weak substrate, lower affinity than for spermidine, 1.3% of the rate with spermidine
-
-
?
acetyl-CoA + N-acetylputrescine
CoA + N1,N4-diacetylputrescine
show the reaction diagram
acetyl-CoA + N1-acetylspermidine
CoA + N1,N8-diacetylspermidine
show the reaction diagram
-
low affinity
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
show the reaction diagram
acetyl-CoA + N1-dansylnorspermine
CoA + N1-acetyl-N1-dansylnorspermine
show the reaction diagram
-
the acetylation reaction proceeds by Bi-Bi mechanism
-
-
?
acetyl-CoA + N1-dansylspermine
CoA + N1-acetyl-N1-dansylspermine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + N1-methyl-1,3-diaminopropane
CoA + ?
show the reaction diagram
-
-
-
?
acetyl-CoA + N8-acetylspermidine
CoA + N1,N8-diacetylspermidine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
show the reaction diagram
-
-
-
?
acetyl-CoA + poly-L-lysine
CoA + acetyl-poly-L-lysine
show the reaction diagram
-
-
-
?
acetyl-CoA + putrescine
CoA + acetylputrescine
show the reaction diagram
-
breakdown of spermidine and putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
show the reaction diagram
acetyl-CoA + putrescine
CoA + N1-acetylputrescine
show the reaction diagram
acetyl-CoA + spermidine
CoA + N1-acetyl-spermidine
show the reaction diagram
acetyl-CoA + spermidine
CoA + N1-acetyl-sym-norspermidine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
show the reaction diagram
acetyl-CoA + spermine
CoA + N1-acetyl-spermine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
show the reaction diagram
acetyl-CoA + sym-norspermidine
CoA + N1-acetyl-sym-norspermidine
show the reaction diagram
acetyl-CoA + sym-norspermine
CoA + N1-acetyl-sym-norspermine
show the reaction diagram
acetyl-CoA + triethylenetetramine
?
show the reaction diagram
chloroacetyl-CoA + spermine
N1-spermine-acetyl-CoA + ?
show the reaction diagram
N1-chloroacetylation of spermine performed by hSSAT protein, pH 7.5 and 2 microM recombinant human SSAT protein at room temperature for one hour, identity of the product confirmed by mass spectrometry
-
-
?
additional information
?
-
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
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
show the reaction diagram
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetyl-spermidine
show the reaction diagram
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
show the reaction diagram
acetyl-CoA + 1,3-diaminopropane
CoA + ?
show the reaction diagram
P48026
-
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
show the reaction diagram
-
reaction occurs in vivo and in vitro, but only in presence of increased enzyme levels, amantadine may be a specific drug substrate for SSAT
-
?
acetyl-CoA + diethylenetriamine
CoA + ?
show the reaction diagram
P48026
-
-
-
?
acetyl-CoA + eIF5A
CoA + acytyl-eIF5A
show the reaction diagram
-
-
selective acetylation of the hypusine and/or deoxyhypusine residue of translation initiation factor eIF5A, resulting in loss of eIF5A activity. Hypusine or deoxyhypusine, as the free amino acid, do not act as a substrate for isoform SSAT1
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
show the reaction diagram
acetyl-CoA + N1-methyl-1,3-diaminopropane
CoA + ?
show the reaction diagram
P48026
-
-
-
?
acetyl-CoA + putrescine
CoA + acetylputrescine
show the reaction diagram
-
breakdown of spermidine and putrescine
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
show the reaction diagram
acetyl-CoA + spermine
CoA + N1-acetylspermine
show the reaction diagram
acetyl-CoA + triethylenetetramine
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
additional information
-
no known cofactors
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-Dephospho-CoA
-
less inhibition than by CoA
6,6-difluorospermidine
-
weak inhibition
acetyl-CoA
-
at high concentrations slight inhibition
amantadine
-
competitively inhibits spermidine acetylation, at 10 mM: complete inhibition
Berenil
Butan-2,3-dione
-
at 10 mM, in presence of borate buffer pH 9.0
CoA
-
strong inhibitor
CoA methyl disulfide
-
very strong inhibitor
diminazene aceturate
-
inhibitor of SSAT-1, does not induce apoptosis
-
hexamethylenediamine
-
30% inhibition
mescaline
-
-
N-acetylputrescine
-
slight, competitive inhibition
N-ethylmaleimide
-
-
N1,N11-bis-(ethyl)-norspermine
-
-
N1-spermine-acetyl-CoA
bisubstrate analogue, bisubstrate inhibition patterns determined, linear, competitive inhibition against sperimidine and acetyl-CoA determined
O-(11-amino-3,8-diaza-1-undecyl)oxime S-(2-oxopropyl)-CoA
-
-
-
O-(11-amino-3,8-diaza-1-undecyl)oxime S-(2-oxopropyl)-D-pantetheine
-
-
-
O-(6-amino-3-aza-1-hexyl)oxime S-(2 oxopropyl)-CoA
-
-
-
O-(6-amino-3-aza-1-hexyl)oxime S-(2-oxopropyl)-D-pantetheine
-
-
-
O-(7-amino-3-aza-1-heptyl)oxime S-(2 oxopropyl)-CoA
-
-
-
O-(7-amino-3-aza-1-heptyl)oxime S-(2-oxopropyl)-D-pantetheine
-
-
-
O-(7-amino-4-aza-1-heptyl)oxime S-(2 oxopropyl)-CoA
-
-
-
O-(7-amino-4-aza-1-heptyl)oxime S-(2-oxopropyl)-D-pantetheine
-
-
-
p-chloromercuribenzoate
pentamethylenediamine
-
30% inhibition
Pentamidine
Phenylglyoxal
-
at 10 mM, in bicarbonate buffer, pH 9.0
S-(2-oxopropyl)-CoA
-
-
-
S-(2-oxopropyl)-D-pantetheine
-
-
-
spermidine
-
0.005 mM, strong inhibition of eIF5A acetylation
spermine
sulfamethazine
-
inhibits spermidine acetylation
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N1,N11-bis(ethyl)-norspermidine
increases SSAT activity, tumor regression analyzed in tumor-bearing transgenic mice expressing SSAT, tumor regression not enhanced by treatment with
-
N1,N11-bis(ethyl)norspermine
-
polyamine analogue, about 300fold activation of wild-type enzyme, 4fold activation of mutant L156F, the compound highly stabilizes the wild-type enzyme preventing it from degradation, while the effect on degradation of the mutant enzyme is smaller
N1,N11-bis-(ethyl)-norspermine
-
induces mRNA and activity of SSAT protein, translation proceeded by competition of a predicted RNA-binding protein
N1,N11-diethylnorspermine
-
polyamine analogue with clinical relevance as an experimental anticancer agent. Treatment of human C-28/I2 chondrocytes rapidly induces spermidine/spermine N1-acetyltransferase and spermine oxidase activities, and down-regulates ornithine decarboxylase. The treatment does not provoke cell death and caspase activation when given alone for 24 h, but causes a caspase-3 and -9 dependent apoptosis in chondrocytes further exposed to cycloheximide. The simultaneous addition of N1,N11-diethylnorspermine and cycloheximide rapidly increases caspase activity in C-28/I2 cells in the absence of spermidine/spermineN1-acetyltransferase and spermine oxidase induction or significant reduction of polyamine levels. Caspase activation induced by N1,N11-diethylnorspermine plus cycloheximide is not prevented by a N1-acetylpolyamine oxidase inhibitor
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.106
1,12-diamino-3,6,9-triazadodecane
-
pH and temperature not specified in the publication
-
0.107 - 1.25
1,3-Diaminopropane
0.1 - 0.44
1,5-Diaminopentane
0.4
1,6-diaminohexane
-
-
1.59
1,7-Diaminoheptane
-
-
0.012
15-deoxyspergualin
-
-
0.0015 - 0.056
acetyl-CoA
2.4
acetylputrescine
-
-
0.41
aminopropylcadaverine
-
pH 9
0.215
D-Glucosamine 6-phosphate
pH 8.0, 30C
0.194
diethylenetriamine
measured at fixed saturating concentrations of acetyl-CoA
0.196
ethylenediamine
measured at fixed saturating concentrations of acetyl-CoA
4.4
N1-acetylspermidine
-
-
0.03 - 0.295
N1-acetylspermine
0.01
N1-dansylnorspermine
-
pH 7.8, 37C, SSAT in hepatoma cells
0.018
N1-dansylspermine
-
pH 7.8, 37C, SSAT in hepatoma cells
1.4
N8-Acetylspermidine
-
-
0.859
poly-L-lysine
pH 8.0, 30C
0.25 - 3
putrescine
0.022 - 2.4
spermidine
0.0037 - 1.7
spermine
0.008 - 0.5
sym-norspermidine
0.083
triethylenetetramine
-
pH and temperature not specified in the publication
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.365 - 0.858
acetyl-CoA
0.1
aminopropylcadaverine
Bacillus subtilis
-
pH 9
1.358
D-Glucosamine 6-phosphate
Streptomyces sp.
D2CFQ9
pH 8.0, 30C
0.12
N1-acetylspermine
Bacillus subtilis
-
pH 9
3.953
poly-L-lysine
Streptomyces sp.
D2CFQ9
pH 8.0, 30C
0.087 - 8.7
spermidine
0.32 - 9
spermine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.17
acetyl-CoA
Streptomyces sp.
D2CFQ9
pH 8.0, 30C
29
24
D-Glucosamine 6-phosphate
Streptomyces sp.
D2CFQ9
pH 8.0, 30C
501
4.6
poly-L-lysine
Streptomyces sp.
D2CFQ9
pH 8.0, 30C
2769
1.5 - 122.2
spermidine
148
1.9 - 62.4
spermine
197
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.738
amantadine
-
-
0.14
BE-333
-
pH 8.0
0.0012 - 0.0042
Berenil
0.03
CGC-11047
-
pH 8.0
0.13
CGC-11048
-
pH 8.0
0.062
CGC-11144
-
pH 8.0
0.022
CGC-11157
-
pH 8.0
0.1
CGC-11158
-
pH 8.0
0.101
CGC-11160
-
pH 8.0
0.021
CGC-11256
-
pH 8.0
0.04
CoA
-
-
1.7
N-acetylputrescine
-
-
0.006
N1-spermine-acetyl-CoA
bisubstrate analogue, linear, competitive inhibition, structure of hSSAT with bound N1-spermine-acetyl-CoA determined
3.5
sulfamethazine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000003 - 0.00008
-
activity in different clones of a transfected rat epidermal cell line expressing the enzyme
0.0000035
-
recombinant EGFP-tagged SSAT in cells
0.00007
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate putrescine; recombinant HEK-293 cells expressing isozyme SSAT-2, substrate putrescine
0.00008
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate N1-acetylspermine; recombinant HEK-293 cells expressing isozyme SSAT-2, substrate N1-acetylspermine
0.0002
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate N1-acetylspermine
0.00023
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermine; recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermine
0.00025
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermidine; recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermidine
0.0004
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate spermine
0.00068
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate norspermidine; recombinant HEK-293 cells expressing isozyme SSAT-2, substrate norspermidine
0.001
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate spermidine
0.0011
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate norspermidine
0.0012
-
recombinant EGFP-tagged SSAT in cells in presence of N'-ethyl-N''-[(cyclopropyl)-methy]-4,8-diazaundecane
0.0058
-
recombinant EGFP-tagged SSAT in cells in presence of N'-ethyl-N''-[(cycloheptyl)methy]-4,8-diazaundecane
0.0106
-
recombinant EGFP-tagged SSAT in cells in presence of N',N''-diethylnorspermine
0.4314
-
-
1.5
-
purified recombinant mutant L156F
26
-
purified recombinant wild-type enzyme
45
-
spermidine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at; assay at
7.4
-
assay at
7.7 - 7.9
-
-
8.5 - 9
-
putrescine
8.5
-
assay at
9 - 9.5
-
spermidine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
about 50% of maximum activity
6.7 - 9.1
activity monitored every 0.3 pH units, bell shaped pH activity profile, depending on ionization state of two groups with apparent pKa values of 7.27 and 8.87
7.6 - 8
-
high conversion rates in the range of
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
about 50% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in breast tumors, SSAT is increased contributing to an increase in acetylated polyamines
Manually annotated by BRENDA team
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
Manually annotated by BRENDA team
cDNA clone of human SSAT
Manually annotated by BRENDA team
-
primary fetal fibroblasts
Manually annotated by BRENDA team
-
the enzyme is inducible in response to 5-fluorouracil or oxaliplatin in parental and drugresistant HCT116 cell lines
Manually annotated by BRENDA team
-
colon cancer cells Caco-2 and HTC-116
Manually annotated by BRENDA team
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
Manually annotated by BRENDA team
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
Manually annotated by BRENDA team
-
melanoma-derived cells C8146C
Manually annotated by BRENDA team
-
TNFalpha can lead to the induction of NFkappaB signaling with a concomitant increase in spermidine/spermine N1-acetyltransferase expression
Manually annotated by BRENDA team
-
A549 and H157. TNFalpha can lead to the induction of NFkappaB signaling with a concomitant increase in spermidine/spermine N1-acetyltransferase expression
Manually annotated by BRENDA team
isozyme SSAT-2; isozyme SSAT-2
Manually annotated by BRENDA team
-
human breast carcinoma cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme, expressed in Escherichia coli DH5alpha, is present at a level of about 2% of the soluble protein
-
Manually annotated by BRENDA team
additional information
-
subcellular localization study, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000 - 40000
-
gel filtration
75000
-
gel filtration
76000
-
gel filtration
115000
-
gel filtration
220000 - 230000
ligand-free enzyme, gel filtration and small-angle X-ray scattering analysis
250000
polyamine-bound enzyme, gel filtration and small-angle X-ray scattering analysis
270000
polyamine-bound enzyme, gel filtration and small-angle X-ray scattering analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * ? + x * 13000, catalytic subunit, at least 2 subunits, gel filtration of enzyme precipitated by (NH4)2SO4
dodecamer
homodimer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
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no posttranslational modification specific to eukaryotes is needed for enzyme activity
phosphoprotein
additional information
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selfacetylation of Lys26 in the presence of acetyl-cCoA and in absence of substrate
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of PaiA in complex with CoA at 1.9A resolution, crystals belong to space group C222(1), with cell parameters of alpha = 39.9 A, beta = 135.8 A and gamma = 132.4 A
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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, 20C, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution
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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
precipitation with polyethylene glycol, high resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA, spermine, and the inhibitor N1,N11-bis-(ethyl)-norspermine
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SSAT bound to a bisubstrate analogue N1-spermine-acetyl-CoA
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three-dimensional crystal structure of SSAT with bound bisubstrate inhibitor, solved at 2.3 A resolution, hanging drop method, data and refinement statistics
SSAT in complex with coenzyme A, with and without bound spermine, hanging drop vapor diffusion method at 4C, crystals of the binary complex between SSAT and CoA are obtained in 20% PEG 8000, 80 mM sodium acetate, 15% glycerol, 2 mM spermine, 1 mM CoA, and 85 mM sodium cacodylate, pH 6.0, 0.001 ml of the protein solution is mixed with 0.01 ml of precipitant solution containing 20% PEG 8000, 50 mM NaCl, 2 mM spermine, 1 mM coenzyme A, 15% glycerol, and 100 mM bicine buffer, pH 9.0. Crystals are obtained at pH 5.0-6.5 over a broad range of precipitant and salt concentrations. Introduction of spermine results in displacement of CoA from the enzyme active site. X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution
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molecular modeling of structure. Both spermidine and spermine should bind at unique position with high specificity
enzyme in ligand-free form or complxed with spermine or spermidine, and/or acetyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.83 A resolution, the enzyme occurs in open and closed conformations
purified enzyme, dodecameric structure in a ligand-free form in three different conformational states, open, intermediate and closed, sitting drop vapor diffusion method, for open state crystals: mixing of 400 nl of 10 mg/ml protein in 100 mM sodium chloride, 10 mM HEPES, pH 7.5, with 400 nl of reservoir solution containing 8% isopropanol and 0.1 M Tris-HCl, pH 8.5, for closed state crystals: mixing of 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, with 0.001 ml of reservoir solution that contains 0.05 M ammonium sulfate, 0.1 M tri-sodium citrate and 15% polyethylene glycol 8000, and for intermediate state crystals: 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, and 0.001 ml of reservoir solution containing 0.01 M calcium chloride, 20% methanol, and 0.1 M Tris-HCl, pH 8.5, 19C, X-ray diffraction structure determination and analysis at 2.38-2.88 A reolution, molecular replacement. All structures are crystallized in C2 space group symmetry and contain six monomers in the asymmetric unit cell. Two hexamers related by crystallographic 2fold symmetry form the SpeG dodecamer. The open and intermediate states have a unique open dodecameric ring
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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stability maximum, rapid fall on either side
487256
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35.5
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crude extract, half-life: 0.75 min
37
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half-life: above 1 h
45
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half-life: 2.2 min, in 50 mM Tris-HCl, pH 7.5, 10 mM spermidine
52
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half-life: 0.5 min, in 50 mM Tris-HCl, pH 7.5, 10 mM spermidine
56
-
half-life: less than 0.5 min
58.2
melting temperature
60
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0.5 min, 90% loss of activity, in 50 mM Tris-HCl, pH 7.5, 10 mM spermidine
85
irreversible heat denaturing
additional information
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very sensitive to heat denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
N1,N11-bis(ethyl)norspermine completely stabilizes the wild-type enzyme, which is degraded within 90 min in absence of N1,N11-bis(ethyl)norspermine, half-life: 22 min, half-life in presence of N1,N11-bis(ethyl)norspermine: 144 h, while for the mutant L156F half-life is 105 min and 154 min, respectively
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N1,N11-diethylnorspermine stabilizes
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native protein conformation is unstable, polyamine analogues such as N1,N12-bis(ethyl)spermine greatly stabilize, conformational changes caused by their binding prevent the efficient polyubiquination of enzyme and therefore its degradation
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PMSF and Brij 35 are essential to prevent rapid loss of activity of the enzyme preparation
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sensitive to incubation in dilute solutions, bovine serum albumin, 0.5 mg/ml, stabilizes
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unstable enzyme, glycerol 10% v/v or bovine serum albumin, 5 mg/ml, partially stabilizes
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unstable enzyme, spermidine stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM Tris-HCl buffer, pH 7.5, 10 mM spermidine, per week, 30% loss of activity
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-22C, per month, 10-16% loss of activity
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-70C, several weeks, stable
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25C, glycerol 10% v/v or bovine serum albumin, 5 mg/ml, more than 22 h, stable
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4C, per day, 5-9% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1027fold; partial
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26fold, partial
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62fold purification of recombinant enzyme, expressed in Escherichia coli DH5alpha
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gel filtration, recombinant protein
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gel filtration, recombinant protein, all purification procedures at 4C
partial
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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recombinant His-tagged wild-type and mutant L156F enzymes from in vitro transcription and translation
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recombinant N-terminally GST- or His6-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography
recombinant N-terminally GST- or His6-tagged enzymes from Escherichia coli strain BL21 by affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and conditional expression of cDNA encoding enzyme in Escherichia coli CAG2242 results in a decrease of endogenous spermidine contents and growth rates
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cloning and expression of cDNA encoding enzyme in Escherichia coli DH5alpha leads to a significant reduction in the cell growth rate
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complete SSAT cDNA is cloned, tetracyclin-regulated cDNA is expressed in MCF-7 human breast carcinoma cells, conditional overexpression lowers polyamine pools, inhibits cell growth and enhances growth sensitivity to certain analogs
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DNA and amino acid sequence determination of isozyme SSAT-2, localization of isozyme SSAT-2 on chromosome 17p13.1, expression of isozyme SSAT-2 in HEK-293 cells; DNA and amino acid sequence determination of isozyme SSAT-2, localization of isozyme SSAT-2 on chromosome 17p13.1, expression of isozyme SSAT-2 in HEK-293 cells; localization of isozyme SSAT-1 on chromosome Xp22
enzyme expression, with or without fused luciferase gene, in HeLa cells possessing a stress-activated protein/extracellular signal-regulated protein kinase, amino acid deprivation upregulates enzyme expression level of 2 different mRNA forms, the effects of different amino acids, especially leucine, arginine, and methionine, are differently high and long-lasting, expression analysis under different conditions, overview
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expressed in Escherichia coli BL21-Gold(DE3)pLysS cells, transformed with pGEX expression vectors
expressed in Escherichia coli, FLAG-tagged SSAT protein and SSAT protein fused to Renilla luciferase
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expressed in Escherichia coli, strains Nova Blue and BL21(DE3), plasmid pET-28a
expression in a rat epidermal cell line, enzyme overexpression in transgenic mice
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expression in Escherichia coli
expression of His-tagged SSAt in Escherichia coli strain BL21(DE3)
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expression of SSAT in HT-29 cells and LoVo cells, two colorectal cancer cell lines, using an adenoviral vector, recombinant enzyme expression causes arrest of cell cycle and cell growth in the S-phase
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expression of SSAT in MGC803 and SGC7901 cells, two gastric cancer cell lines, using an adenoviral vector, recombinant enzyme expression inhibits cell growth in vitro and in vivo, Ad-SSAT arrests gastric cancer cells in S phase, mediated through downregulation of the cyclin A-E2F signaling pathway, polyamine contents in the cells, overview
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expression of the L156F mutant enzyme in C55.7Res cells, in vitro transcription and translation of His-tagged wild-type and mutant L156F enzymes
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full-length cDNA is cloned and expressed in Escherichia coli M15, generation of a transgenic mouse line systemically overexpressing SSAT, overexpression alters polyamine pools and sensitize cells to the antiproliferative activity of N1,N11-diethylnorspermine
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gene Sat1, located on the X chromosome at Xp22.1, DNA and amino acid sequence analysis, genetic structure, overview
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gene sat1, quantitative one-step real-time PCR enzyme expression analysis
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gene speG, recombinant enzyme expression in Escherichia coli strain BL21(DE3)
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gene ssat1, sequence comparison, expression profile, and phylogenetic analysis of ssat-like genes, recombinant expression of N-terminally GST- or His6-tagged enzyme in Escherichia coli strain BL21, recombinant expression in HEK-293T cells
genes ssat1a, ssat1b, and ssat1c, sequence comparisons, expression profiles and phylogenetic analysis of ssat-like genes, translational regulatory mechanism analysis, recombinant expression of N-terminally GST- or His6-tagged enzymes in Escherichia coli strain BL21, recombinant expression of N-terminally GST- or His6-tagged enzymes in HEK-293T cells
plasmid pSAT9.3, containing SSAT cDNA cloned into Bluescript vector, is used to express the protein from the T7 promoter using rabbit reticulocyte TNT coupled expression system
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recombinant overexpression of the enzyme in enzyme-deficient and wild-type mice using the endogenous enzyme promoter, quantitative PCR expression analysis
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SAT1 gene, located on the X chromosome, genotyping
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SAT1, microarray expression analysis in brains of control individuals and depressed individuals who have died by suicide, overview
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SSAT gene is cloned, tetracyclin-regulated gene lacking the 5-flanking region is expressed in MCF-7 human breast carcinoma cells, conditional overexpression lowers polyamine pools, inhibits cell growth and enhances growth sensitivity to certain analogs
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SSAT overexpression in prostate cancer cells leads to a massive increase in intracellular and extracellular acetylated spermidine and to a 6-20fold increase in biosynthetic enzyme activities, overview. In the presence of 4-fluoro-ornithine, SSAT overexpression leads to the sequential appearance of fluorinated putrescine, spermidine, acetylated spermidine, and spermine
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transduction of HEK-293T cells with an adenovirus encoding the enzyme and enzyme overexpression
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transfection of the SSAT repressed C13 cells with two expression vectors driving human SSAT overexpression by diverse promoters. SSAT overexpression inhibits cell growth and enhances growth sensitivity to N1,N12-bis(ethyl)spermine in C13 cells
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transgenic CD2F1 mice overexpressing SSAT
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transient expression of EGFP-tagged SSAT in SSAT-deficient mouse fetal fibroblasts in cytosol and nucleus. The presence of SSAT-EGFP leads to a 9fold induction in SSAT activity in transfected untreated cells when compared with the cells transfected with EGFP
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
antitumorigenicity of upregulated SSAT
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induction of enzyme SSAT with alpha-methylspermidine disturbs wild-type osteoblastogenesis
induction of SSAT gene expression by combined quinoxalines and spermidine analogue treatment, overview. The cDDP-resistant human ovarian cell line, A2780/CP, shows defective expression and inducibility of SSAT by Spm analogues, when compared to the sensitive counterpart A2780
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lithium induces enzyme expression in low and high risk groups for suicide commitment as well as in controls, but it has no effect in suicide completers. Differences in lithium-induced increase