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Information on EC 3.5.4.36 - mRNA(cytosine6666) deaminase and Organism(s) Oryctolagus cuniculus and UniProt Accession P47855

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EC Tree
IUBMB Comments
The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine6666 to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site .
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Oryctolagus cuniculus
UNIPROT: P47855
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Word Map
  • 3.5.4.36
  • cytidine
  • polypeptide-like
  • deamination
  • deaminases
  • apobecs
  • hypermutation
  • editosome
  • c-to-u
  • mooring
  • apob48
  • apob100
  • rna-specific
  • unedited
  • mcardle
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
cytosine6666 in apolipoprotein B mRNA
+
=
uracil6666 in apolipoprotein B mRNA
+
Synonyms
apobec-1, apolipoprotein b mrna editing enzyme, apob mrna-editing enzyme catalytic polypeptide 1, apo b messenger rna editing protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
APOBEC1
catalytic component of an RNA-editing complex
SYSTEMATIC NAME
IUBMB Comments
mRNA(cytosine6666) aminohydrolase
The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine6666 to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cytosine6666 in apolipoprotein B mRNA + H2O
uracil6666 in apolipoprotein B mRNA + NH3
show the reaction diagram
auxiliary proteins of the apoB mRNA editing complex, which are essential for editing activity, exist in organs devoid of significant apoB mRNA editing or apoB synthesis
-
-
?
cytosine6666 in apolipoprotein B mRNA + H2O
uracil6666 in apolipoprotein B mRNA + NH3
show the reaction diagram
-
apolipoprotein B mRNA editing at nucleotide 6666 converts cytidine to uridine, transforming the codon for glutamine-2153 to a termination codon
-
-
?
additional information
?
-
APOBEC1 possesses antiviral activity. It is capable of inhibiting the infectivity of various lentiviruses in tissue culture models
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cytosine6666 in apolipoprotein B mRNA + H2O
uracil6666 in apolipoprotein B mRNA + NH3
show the reaction diagram
-
apolipoprotein B mRNA editing at nucleotide 6666 converts cytidine to uridine, transforming the codon for glutamine-2153 to a termination codon
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
the enzyme requires zinc for its catalytic activity. A zinc motif is essential for catalytic activity. His61, Cys93, and Cys96 are essential for editing activity, probably because they coordinate zinc
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
unlike their human counterparts, APOBEC1 in a wide range of mammalian species may function as a defense mechanism regulating retroelements
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ABEC1_RABIT
236
0
27719
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
calculated from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C93A
the mutant retains 4% of wild-type editing activity
C96A
mutant lacks activity
E63Q
inactive mutant enzyme. The ability of the mutant proteins to restrict the infectivity of wild-type and DELTAvif viruses are severely, but not completely impaired
H61A
mutant lacks activity
H61C
mutant shows 80% of wild-type editing activity
P92A
the mutant retains 18% of wild-type editing activity
V62A
the mutant retains 89% of wild-type editing activity
additional information
the truncated mutant form of the rabbit REPR that lacks the COOH-terminal one-third containing the putative leucine-rich motif is catalytically inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, D.F.; Poksay, K.S.; Innerarity, T.L.
The mechanism for apo-B mRNA editing is deamination
Biochem. Biophys. Res. Commun.
195
1204-1210
1993
Oryctolagus cuniculus
Manually annotated by BRENDA team
Yamanakam, S.; Poksay, K.S.; Balestra, M.E.; Zeng, G.Q.; Innerarity, T.L.
Cloning and mutagenesis of the rabbit ApoB mRNA editing protein. A zinc motif is essential for catalytic activity, and noncatalytic auxiliary factor(s) of the editing complex are widely distributed
J. Biol. Chem.
269
21725-21734
1994
Oryctolagus cuniculus (P47855)
Manually annotated by BRENDA team
Ikeda, T.; Ohsugi, T.; Kimura, T.; Matsushita, S.; Maeda, Y.; Harada, S.; Koito, A.
The antiretroviral potency of APOBEC1 deaminase from small animal species
Nucleic Acids Res.
36
6859-6871
2008
Mesocricetus auratus (Q9EQP0), Mus musculus (P51908), Mustela putorius furo (B2NIW5), Oryctolagus cuniculus (P47855), Rattus norvegicus (P38483)
Manually annotated by BRENDA team