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Information on EC 3.5.4.35 - tRNA(cytosine8) deaminase and Organism(s) Methanopyrus kandleri and UniProt Accession Q8TWU6

for references in articles please use BRENDA:EC3.5.4.35
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IUBMB Comments
The enzyme from Methanopyrus kandleri specifically catalyses the deamination of cytosine at position 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
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This record set is specific for:
Methanopyrus kandleri
UNIPROT: Q8TWU6
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The taxonomic range for the selected organisms is: Methanopyrus kandleri
The expected taxonomic range for this enzyme is: Methanopyrus kandleri
Reaction Schemes
cytosine8 in tRNA
+
=
uracil8 in tRNA
+
Synonyms
cdat8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
tRNA(cytosine8) aminohydrolase
The enzyme from Methanopyrus kandleri specifically catalyses the deamination of cytosine at position 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
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 SUBSTRATE
NATURAL 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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
gel filtration
SUBUNIT
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Randau, L.; Stanley, B.; Kohlway, A.; Mechta, S.; Xiong, Y.; Soell, D.
A cytidine deaminase edits C to U in transfer RNAs in archaea
Science
324
657-659
2009
Methanopyrus kandleri (Q8TWU6), Methanopyrus kandleri
Manually annotated by BRENDA team