Information on EC 3.5.4.B9 - cytosine deaminase APOBEC3G and Organism(s) Homo sapiens

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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.4.B9
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
cytosine deaminase APOBEC3G
-
SYSTEMATIC NAME
IUBMB Comments
single-stranded DNA cytosine aminohydrolase APOBEC3G
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
in ssDNA
-
-
?
5'-AAAGAGAAAGAGAAACCCAAAGAGGAAAGGTGAGGAGAA-3' + H2O
5'-AAAGAGAAAGAGAAACCUAAAGAGGAAAGGTGAGGAGAA-3' + NH3
show the reaction diagram
-
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
show the reaction diagram
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
show the reaction diagram
-
-
-
-
?
TTTCCCCGC + H2O
TTTCCUCGC + NH3
show the reaction diagram
-
sequence with highest deamination rate
-
-
?
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
2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
show the reaction diagram
-
in ssDNA
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
show the reaction diagram
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
NaCl
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(12bS)-5,6,6a,7,8,12b-hexahydrobenzo[a]phenanthridine-10,11-diol
-
-
(1R,2S)-2-(methylamino)-1-phenylpropan-1-ol
-
-
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
-
-
(2S)-3-(3,4-dihydroxyphenyl)-2-hydrazinyl-2-methylpropanoic acid
-
-
(3,4-dihydroxyphenyl)acetic acid
-
-
(5E)-N-methyl-2,3-diphenyl-1,2,4-thiadiazol-5(2H)-imine
-
-
(6aR)-6-(prop-2-en-1-yl)-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
-
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
-
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-2,10,11-triol
-
-
(6aR)-6-propyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
-
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[2-[(pyridin-4-yl)sulfanyl]acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
-
-
2-amino-3-(2,4,5-trihydroxyphenyl)propanoic acid
-
-
2-Iodoacetamide
-
-
2-phenyl-1,2-benzoselenazol-3(2H)-one
-
-
2-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-hydroxy-4H-pyran-4-one
-
-
2-[methyl(nitroso)amino]benzene-1,4-diol
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-yl)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
-
-
4,4'-(2,3-dimethylbutane-1,4-diyl)dibenzene-1,2-diol
-
-
4-(4,5,6,7-tetrahydrothieno[2,3-c]pyridin-4-yl)benzene-1,2-diol
-
-
4-amino-5-methyl-1,2,4-triazole-3-thiol
-
-
4-[(2-sulfanyl-1H-imidazol-1-yl)methyl]phenol
-
-
4-[(4-bromobenzylidene)amino]-1,2,4-triazole-3-thiol
-
MN256.0105, 99% inhibition at 0.02 mM
4-[(4-methoxybenzylidene)amino]-5-methyl-1,2,4-triazole-3-thiol
-
-
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
-
-
4-[methyl(nitroso)amino]benzene-1,2-diol
-
-
6-amino-5,6,7,8-tetrahydronaphthalene-2,3-diol
-
-
aurothio-beta-D-glucose
-
-
benzene-1,4-diol
-
-
cephapirin
-
-
cyclohexa-2,5-diene-1,4-dione
-
-
methyl 2-amino-3-(3,4-dihydroxyphenyl)propanoate
-
-
N-(3-thio-5-methyl-1,2,4-triazol-4-yl)benzamide
-
-
N-[(4bS,8R,8aS)-7-(cyclopropylmethyl)-1,8a-dihydroxy-5,6,7,8,8a,9,14,14b-octahydro-4,8-methano[1]benzofuro[2,3-a]pyrido[4,3-b]carbazol-11-yl]guanidine
-
-
N-[2-(3,4-dihydroxyphenyl)ethyl]acetamide
-
-
p-chloromercuribenzoate
-
-
tetrasodium 3-[(E)-[4-formyl-5,6-dihydroxy-3-[(phosphonatoperoxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01615 - 0.3944
cytosine in single-stranded viral DNA
-
additional information
additional information
-
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000083 - 0.008
cytosine in single-stranded viral DNA
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.24
cytosine in single-stranded viral DNA
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00059
(12bS)-5,6,6a,7,8,12b-hexahydrobenzo[a]phenanthridine-10,11-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0013
(1R,2S)-2-(methylamino)-1-phenylpropan-1-ol
Homo sapiens
-
at pH 7.8 and 37C
0.085
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
Homo sapiens
-
at pH 7.8 and 37C
0.0053
(2S)-3-(3,4-dihydroxyphenyl)-2-hydrazinyl-2-methylpropanoic acid
Homo sapiens
-
at pH 7.8 and 37C
0.019
(3,4-dihydroxyphenyl)acetic acid
Homo sapiens
-
at pH 7.8 and 37C
0.029
(5E)-N-methyl-2,3-diphenyl-1,2,4-thiadiazol-5(2H)-imine
Homo sapiens
-
at pH 7.8 and 37C
0.0029
(6aR)-6-(prop-2-en-1-yl)-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0013
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0017
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-2,10,11-triol
Homo sapiens
-
at pH 7.8 and 37C
0.0064
(6aR)-6-propyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0075
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[2-[(pyridin-4-yl)sulfanyl]acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Homo sapiens
-
at pH 7.8 and 37C
0.027
1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
Homo sapiens
-
at pH 7.8 and 37C
0.004
2-amino-3-(2,4,5-trihydroxyphenyl)propanoic acid
Homo sapiens
-
at pH 7.8 and 37C
0.003
2-Iodoacetamide
Homo sapiens
-
at pH 7.8 and 37C
0.0028
2-phenyl-1,2-benzoselenazol-3(2H)-one
Homo sapiens
-
at pH 7.8 and 37C
0.002
2-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-hydroxy-4H-pyran-4-one
Homo sapiens
-
at pH 7.8 and 37C
0.00043
2-[methyl(nitroso)amino]benzene-1,4-diol
Homo sapiens
-
at pH 7.8 and 37C
0.00049
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-yl)methanediyl]bis(6-hydroxybenzoic acid)
Homo sapiens
-
at pH 7.8 and 37C
0.0034
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
Homo sapiens
-
at pH 7.8 and 37C
0.0088
4,4'-(2,3-dimethylbutane-1,4-diyl)dibenzene-1,2-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0013
4-(4,5,6,7-tetrahydrothieno[2,3-c]pyridin-4-yl)benzene-1,2-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0061
4-amino-5-methyl-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37C
0.0035
4-[(2-sulfanyl-1H-imidazol-1-yl)methyl]phenol
Homo sapiens
-
at pH 7.8 and 37C
0.0043
4-[(4-bromobenzylidene)amino]-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37C
0.0039
4-[(4-methoxybenzylidene)amino]-5-methyl-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37C
0.0018
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0091
4-[methyl(nitroso)amino]benzene-1,2-diol
Homo sapiens
-
at pH 7.8 and 37C
0.0007
6-amino-5,6,7,8-tetrahydronaphthalene-2,3-diol
Homo sapiens
-
at pH 7.8 and 37C
0.00036
aurothio-beta-D-glucose
Homo sapiens
-
at pH 7.8 and 37C
0.0026
benzene-1,4-diol
Homo sapiens
-
at pH 7.8 and 37C
0.013
cephapirin
Homo sapiens
-
at pH 7.8 and 37C
0.00017
cyclohexa-2,5-diene-1,4-dione
Homo sapiens
-
at pH 7.8 and 37C
0.013
methyl 2-amino-3-(3,4-dihydroxyphenyl)propanoate
Homo sapiens
-
at pH 7.8 and 37C
0.0082
N-(3-thio-5-methyl-1,2,4-triazol-4-yl)benzamide
Homo sapiens
-
at pH 7.4 and 37C
0.0064
N-[(4bS,8R,8aS)-7-(cyclopropylmethyl)-1,8a-dihydroxy-5,6,7,8,8a,9,14,14b-octahydro-4,8-methano[1]benzofuro[2,3-a]pyrido[4,3-b]carbazol-11-yl]guanidine
Homo sapiens
-
at pH 7.8 and 37C
0.00045
N-[2-(3,4-dihydroxyphenyl)ethyl]acetamide
Homo sapiens
-
at pH 7.8 and 37C
0.00013
p-chloromercuribenzoate
Homo sapiens
-
at pH 7.8 and 37C
0.0056
tetrasodium 3-[(E)-[4-formyl-5,6-dihydroxy-3-[(phosphonatoperoxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonate
Homo sapiens
-
at pH 7.8 and 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
assay at
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states
88000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer or dimer
-
x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
carboxy-terminal deaminase domain 2 of APOBEC3G (residues 197-380), hanging drop vapor diffusion method, using 100 mM MES, pH 6.5, 40% (w/v) PEG 200, at 18C
-
head-to-tail dimer of the A3G catalytic deamination domain A3G-CD2, sitting drop vapor diffusion method, using 0.1 M sodium citrate tribasic dehydrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) polyethylene glycol 4000
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and MonoQ column chromatography
-
glutathione-Sepharose resin column chromatography and DEAE FF column chromatography
-
Ni Sepharose resin column chromatography
-
Ni-NTA column chromatography and Superdex75 gel filtration
-
Superdex 75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in baculovirus-infected sf9 insect cells
-
expressed in Escherichia coli BL21(DE3) cells and in Sf9 insect cells
-
expressed in Escherichia coli BL21(DE3/RIL) cells
-
expressed in Escherichia coli Rosetta(DE3)plys and BW310 cells
-
expressed in HEK-293 cells
-
expressed in Sf9 insect cells
-
expression of activation-induced deaminase, i.e. AID, and APOBEC3G in Escherichia coli strain BW310 and in human HEK293T cells
-
glutathione S-transferase-tagged enzyme is expressed in Escherichia coli
-
incorporation of hA3G CD1 and CD2 domain mutants into HIV-1. Cotransfection of plasmids coding HIV-1 vif and plasmids containing either wild-type or mutant hA3G in 293T cells
-
the carboxyl-terminal catalytic domain is expressed in Escherichia coli BL-21 DE3 codon+RIL cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C243A/C321A/C356A
-
the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 19%
C288A/C291A
-
the mutant enzyme shows about 18% activity compared to the wild type enzyme
C321A
-
the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 21%
C97A/C100A
-
the mutant enzyme shows about 18% activity compared to the wild type enzyme
D264A
-
the variant has 5% of the catalytic efficiency of the wild type protein
D316R/D317R
D370A
-
the variant has 16% of the catalytic efficiency of the wild type protein
F126A/W127A
F202A
-
the mutation causes a decrease of the enzyme activity
F241K
-
the mutation causes a decrease of the enzyme activity
F268A
-
the variant has 25% of the catalytic efficiency of the wild type protein
F298A
-
the mutant shows about 10% deamination activity compared to the wild type enzyme
H186R
-
the clinical mutant is associated with high viral loads. The mutant has altered DNA scanning properties in sliding which results in decreased abilities to induce mutagenesis during reverse transcription. The mutant retains a strong preference for deamination of the 5'-CCC motif and exhibits a processivity factor that is similar to native enzym
H248G
-
the variant has 158% of the catalytic efficiency of the wild type protein
H250A
-
the variant has 266% of the catalytic efficiency of the wild type protein
H257A
-
the mutant enzyme shows about 10% activity compared to the wild type enzyme
H81A
-
the mutant enzyme shows about 25% activity compared to the wild type enzyme
I314A/Y315A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
L235A
-
the mutation causes a decrease of the enzyme activity
L235K
-
the mutation causes a decrease of the enzyme activity
L242A
-
the mutation causes a decrease of the enzyme activity
L242K
-
the mutation causes a decrease of the enzyme activity
N244A
-
the mutant shows no deamination activity
P210A
-
the variant has 1% of the catalytic efficiency of the wild type protein
P210G
-
the variant has 10% of the catalytic efficiency of the wild type protein
Q245A
-
the mutation nearly abolishes the catalytic efficiency to 5% compared to the wild type protein
Q380A
-
the variant has 68% of the catalytic efficiency of the wild type protein
R213E
-
the mutant shows about 3% deamination activity compared to the wild type enzyme
R215E
-
the mutant shows no deamination activity
R256A
-
the mutation nearly abolishes the catalytic efficiency to 1% compared to the wild type protein
R256E
-
the mutant shows about 3% deamination activity compared to the wild type enzyme
R313A/D316A/D317A/Q318A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
R313E/R320D
-
the mutant shows no deamination activity and about 75% single-stranded DNA binding compared to the wild type enzyme
R374A
-
the variant has 3% of the catalytic efficiency of the wild type protein
R374E/R376D
-
the mutant shows less than 10% deamination activity and about 50% single-stranded DNA binding compared to the wild type enzyme
R376A
-
the variant has 15% of the catalytic efficiency of the wild type protein
T203A
-
the mutation causes a decrease of the enzyme activity
V233A
-
the mutation causes a decrease of the enzyme activity
V233K
-
the mutation causes a decrease of the enzyme activity
W232A
-
the mutation causes a decrease of the enzyme activity
W285A
-
the mutant shows no deamination activity
Y124A/Y125A
-
site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa
Y315A
-
the mutant shows no deamination activity
additional information