Information on EC 3.5.4.35 - tRNA(cytosine8) deaminase

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The expected taxonomic range for this enzyme is: Methanopyrus kandleri

EC NUMBER
COMMENTARY hide
3.5.4.35
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RECOMMENDED NAME
GeneOntology No.
tRNA(cytosine8) deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cytosine8 in tRNA + H2O = uracil8 in tRNA + NH3
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tRNA(cytosine8) aminohydrolase
The enzyme from Methanopyrus kandleri specifically catalyses the deamimation of cytosine at poition 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cytosine8 in tRNA + H2O
uracil8 in tRNA + NH3
show the reaction diagram
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
cytosine8 in tRNA + H2O
uracil8 in tRNA + NH3
show the reaction diagram
Q8TWU6
all canonical tRNAs have a uridine at position 8, involved in maintaining tRNA tertiary structure. The hyperthermophilic archaeon Methanopyrus kandleri harbors 30 (out of 34) tRNA genes with cytidine at position 8. The enzyme catalyzes C-to-U editing at this location. The presence of this C-to-U editing enzyme guarantees the proper folding and functionality of all Methanopyrus kandleri tRNAs
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion. The structure of the enzyme is solved in two different crystal forms. In each form, the asymmetric unit is composed of two identical CDAT8 dimers
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli