BRENDA - Enzyme Database
show all sequences of 3.5.4.B9

Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain

Feng, Y.; Chelico, L.; J. Biol. Chem. 286, 11415-11426 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Sf9 insect cells
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
F126A/W127A
the mutant has altered DNA scanning properties in jumping which results in decreased abilities to induce mutagenesis during reverse transcription. The mutant demonstrates a stronger preference than native enzyme for C residues at the 5'-ssDNA end and is processive
Homo sapiens
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
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cytosine in single-stranded viral DNA + H2O
Homo sapiens
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
uracil in single-stranded viral DNA + NH3
-
-
?
additional information
Homo sapiens
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
-
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cytosine in single-stranded viral DNA + H2O
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
722698
Homo sapiens
uracil in single-stranded viral DNA + NH3
-
-
-
?
additional information
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
722698
Homo sapiens
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Sf9 insect cells
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F126A/W127A
the mutant has altered DNA scanning properties in jumping which results in decreased abilities to induce mutagenesis during reverse transcription. The mutant demonstrates a stronger preference than native enzyme for C residues at the 5'-ssDNA end and is processive
Homo sapiens
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
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cytosine in single-stranded viral DNA + H2O
Homo sapiens
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
uracil in single-stranded viral DNA + NH3
-
-
?
additional information
Homo sapiens
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cytosine in single-stranded viral DNA + H2O
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
722698
Homo sapiens
uracil in single-stranded viral DNA + NH3
-
-
-
?
additional information
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
722698
Homo sapiens
?
-
-
-
-
General Information
General Information
Commentary
Organism
physiological function
the enzyme restricts replication of HIV-1 by inducing viral genome mutagenesis through deamination of cytosine to uracil on HIV-1 cDNA processively through jumping and sliding. The jumping and sliding of Apo3G is needed for efficient mutational inactivation of HIV-1
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme restricts replication of HIV-1 by inducing viral genome mutagenesis through deamination of cytosine to uracil on HIV-1 cDNA processively through jumping and sliding. The jumping and sliding of Apo3G is needed for efficient mutational inactivation of HIV-1
Homo sapiens
Other publictions for EC 3.5.4.B9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734319
Lu
Crystal structure of DNA cytid ...
Homo sapiens
J. Biol. Chem.
290
4010-4021
2015
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12
12
735015
Zhu
Host APOBEC3G protein inhibits ...
Homo sapiens
PLoS ONE
10
e0121608
2015
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721999
Jaszczur
AID and Apobec3G haphazard dea ...
Homo sapiens
Cell. Mol. Life Sci.
70
3089-3108
2013
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734795
Holtz
APOBEC3G cytosine deamination ...
Homo sapiens
Nucleic Acids Res.
41
6139-6148
2013
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718465
Li
First-in-class small molecule ...
Homo sapiens
ACS Chem. Biol.
7
506-517
2012
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1
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34
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5
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34
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720014
Senavirathne
Single-stranded DNA scanning a ...
Homo sapiens
J. Biol. Chem.
287
15826-15835
2012
1
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721668
Shlyakhtenko
Nanoscale structure and dynami ...
Homo sapiens
Biochemistry
51
6432-6440
2012
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722064
Olson
Small-molecule APOBEC3G DNA cy ...
Homo sapiens
ChemMedChem
8
112-117
2012
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723071
Sadler
APOBEC3G contributes to HIV-1 ...
Homo sapiens
J. Virol.
84
7396-7404
2012
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1
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1
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723754
Monajemi
Emerging complexities of APOBE ...
Homo sapiens
Retrovirology
9
35
2012
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1
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719945
Demorest
Phosphorylation directly regul ...
Homo sapiens, Mus musculus
J. Biol. Chem.
286
26568-26575
2011
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2
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7
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721103
Li
Functional analysis of the two ...
Homo sapiens
Virology
414
130-136
2011
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722698
Feng
Intensity of deoxycytidine dea ...
Homo sapiens
J. Biol. Chem.
286
11415-11426
2011
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2
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712428
Chelico
Structural model for deoxycyti ...
Homo sapiens
J. Biol. Chem.
285
16195-16205
2010
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5
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719342
Carpenter
Determinants of sequence-speci ...
Homo sapiens
DNA Repair
9
579-587
2010
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722114
Furukawa
Structure, interaction and rea ...
Homo sapiens
EMBO J.
28
440-451
2009
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722665
Rausch
Dissecting APOBEC3G substrate ...
Homo sapiens
J. Biol. Chem.
284
7047-7058
2009
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723261
Holden
Crystal structure of the anti- ...
Homo sapiens
Nature
456
121-124
2008
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722104
Pham
DNA deaminases AID and APOBEC3 ...
Homo sapiens
DNA Repair
6
689-692
2007
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722103
Coker
The nuclear DNA deaminase AID ...
Homo sapiens
DNA Repair
6
235-243
2006
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1
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723256
Chelico
APOBEC3G DNA deaminase acts pr ...
Homo sapiens
Nat. Struct. Mol. Biol.
13
392-399
2006
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1
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723285
Suspene
APOBEC3G is a single-stranded ...
Homo sapiens
Nucleic Acids Res.
32
2421-2429
2004
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723260
Zhang
The cytidine deaminase CEM15 i ...
Homo sapiens
Nature
424
94-98
2003
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