3.5.4.1: cytosine deaminase
This is an abbreviated version!
For detailed information about cytosine deaminase, go to the full flat file.
Word Map on EC 3.5.4.1
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3.5.4.1
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cytidine
-
deaminases
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5-fluorocytosine
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deamination
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prodrugs
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virion
-
hypermutation
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viruses
-
5-fluorouracil
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apolipoprotein
-
retroviruses
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suicide
-
uracil
-
retroviral
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apobecs
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single-stranded
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antiretroviral
-
polypeptide-like
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mrna-editing
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g-to-a
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bystander
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activation-induced
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retrotransposons
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anti-hiv-1
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proviral
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retroelements
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lentiviruses
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encapsidation
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ganciclovir
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deoxycytidine
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retrotransposition
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ssdna
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fiv
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samhd1
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cullin
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minus-strand
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replication-competent
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gene-directed
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sivmac
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medicine
-
line-1
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hsv-tk
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vpr
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gdept
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non-ltr
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molecular biology
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xenotropic
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analysis
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pharmacology
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biotechnology
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trim5alpha
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diagnostics
-
proviruses
-
nickase
-
agriculture
-
single-cycle
-
elongins
- 3.5.4.1
- cytidine
- deaminases
- 5-fluorocytosine
-
deamination
-
prodrugs
- virion
-
hypermutation
- viruses
- 5-fluorouracil
-
apolipoprotein
- retroviruses
-
suicide
- uracil
-
retroviral
-
apobecs
-
single-stranded
-
antiretroviral
-
polypeptide-like
-
mrna-editing
-
g-to-a
-
bystander
-
activation-induced
-
retrotransposons
-
anti-hiv-1
-
proviral
-
retroelements
- lentiviruses
-
encapsidation
- ganciclovir
- deoxycytidine
-
retrotransposition
- ssdna
- fiv
- samhd1
-
cullin
-
minus-strand
-
replication-competent
-
gene-directed
- sivmac
- medicine
-
line-1
-
hsv-tk
- vpr
-
gdept
-
non-ltr
- molecular biology
-
xenotropic
- analysis
- pharmacology
- biotechnology
- trim5alpha
- diagnostics
- proviruses
-
nickase
- agriculture
-
single-cycle
-
elongins
Reaction
Synonyms
A3DE, APOBEC1, APOBEC3, APOBEC3G, CD, CDA, CDase, codA, CodA protein, Cytosine aminohydrolase, cytosine deaminase, cytosine deaminase I, cytosine deaminase II, cytosine deaminase P, cytosine deaminase S, cytosine deaminase Y, Fca1p, FCY1, isocytosine deaminase, yCD, Zn2+CDase
ECTree
3.5.4.1 cytosine deaminaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.5.4.1 - cytosine deaminase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BaCl2
CaCl2
Fe2+
FeCl3
MnCl2
Zn2+
Fe2+
bound to the active site, the metal ion coordinates a hydroxyl nucleophile, binding structure, overview
Zn2+
-
bound to the enzyme, below 0.2 mol per mol of subunit, reconstitution of apoenzyme
Zn2+
1 metal ion is tightly bound to the active site, binding structure modeling, Fourier mapping
Zn2+
-
ligands are two cysteines, a histidine, and one water molecule
Zn2+
residues His62, Cys91, and Cys94 are very important in coordinating the zinc cation
