3.5.4.38: single-stranded DNA cytosine deaminase
This is an abbreviated version!
For detailed information about single-stranded DNA cytosine deaminase, go to the full flat file.
Word Map on EC 3.5.4.38
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3.5.4.38
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apobec3s
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deamination
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hypermutation
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deaminases
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immunoglobulin
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uracil
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viruses
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apolipoprotein
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retroviruses
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diversification
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ige
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virion
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polypeptide-like
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retroviral
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mrna-editing
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retrotransposons
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antiretroviral
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retroelements
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vif-deficient
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anti-hiv-1
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retrotransposition
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class-switching
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glycosylase
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lentiviruses
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uracil-dna
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line-1
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proviral
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vif-mediated
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aid-dependent
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cccdna
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aid-induced
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abasic
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c-to-u
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encapsidation
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translesion
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r-loops
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sivmac
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molecular biology
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samhd1
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medicine
- 3.5.4.38
- apobec3s
-
deamination
-
hypermutation
- deaminases
- immunoglobulin
- uracil
- viruses
-
apolipoprotein
- retroviruses
-
diversification
- ige
- virion
-
polypeptide-like
-
retroviral
-
mrna-editing
-
retrotransposons
-
antiretroviral
-
retroelements
-
vif-deficient
-
anti-hiv-1
-
retrotransposition
-
class-switching
- glycosylase
- lentiviruses
-
uracil-dna
-
line-1
-
proviral
-
vif-mediated
-
aid-dependent
-
cccdna
-
aid-induced
-
abasic
-
c-to-u
-
encapsidation
-
translesion
-
r-loops
-
sivmac
- molecular biology
- samhd1
- medicine
Reaction
Synonyms
A3F, activation-induced cytidine deaminase, activation-induced deaminase, AICDA, AID, APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, APOBEC3H, APOBEC3Z1, CDA1, single-stranded (ss)DNA deoxycytidine deaminase, ssDNA cytidine deaminase
ECTree
3.5.4.38 single-stranded DNA cytosine deaminaseAdvanced search results
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Engineering on EC 3.5.4.38 - single-stranded DNA cytosine deaminase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E58Q/C87A/C90A
the mutant enzyme does not bind to single-stranded DNA at all, though it retains some binding to RNA
E72D
mutant is moderately impaired in a ssDNA deamination assay but capable of RNA deamination
G56N
mutation at the N-terminus end of loop-3 does not bestow deamination activity
H248S/H250S
increase in the concentration of zinc does not increase deamination activity
K352A/K355A/K358A
the product formation of the mutant enzyme can not reach saturation even when the maximum protein concentration is obtained
Y333A
the product formation of the mutant enzyme can not reach saturation even when the maximum protein concentration is obtained
S38A
S3A
purified recombinant mutant enzyme S3A and wild-type have similar deamination activities on an ssDNA substrate in vitro. AID-/- B cells expressing AIDS3A show a consistently higher percentage of class-switched IgG1-expressing B cells than control enzyme. Mutating S3 to A does not alter catalysis but does result in increased AID activity in class switch recombination
S3D
AID-/- B cells expressing AID-S3D show a consistently higher percentage of class-switched IgG1-expressing B cells than control enzyme. Mutating S3 to A does not alter catalysis but does result in increased AID activity in class switch recombination
T140A
mutation does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo
additional information
S38A
mutant form of activation-induced cytidine deaminase that retains similar catalytic activity on ssDNA as wild-type enzyme. The AIDS38A mutant protein is significantly compromised in its ability to mediate somatic hypermutation SHM. B cells homozygous for the AIDS38A mutation show substantially impaired class switch recombination and Ig somatic hypermutation, correlating with inability of AIDS38A to interact with endogenous replication protein A. Mice haploinsufficient for AIDS38A have more severely impaired class switch recombination when compared with mice haploinsufficient for AIDWT, with class switch recombination levels reduced to nearly background levels. These results unequivocally demonstrate that integrity of the AID S38 phosphorylation site is required for normal class switch recombination and Ig somatic hypermutation in mice and support a role for AID phosphorylation at S38 and replication protein A interaction in regulating class switch recombination and Ig somatic hypermutation
S38A
mutation does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo
S38A
the kinetics of single-stranded DNA deaminase activity for wild-type and S38A mutant enzyme are comparable
S38A
the mutant enzyme shows dimished somatic hypermutation activity on artificial and physiological DNA targets
additional information
construction of segment swaps between activation-induced deaminase (AID) and APOBEC3G and determination of their mutational sequence specificity
additional information
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construction of segment swaps between activation-induced deaminase (AID) and APOBEC3G and determination of their mutational sequence specificity
