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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The expected taxonomic range for this enzyme is: Methanopyrus kandleri
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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.
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
the enzyme is specific for C deamination at position 8, requires only the acceptor stem hairpin for activity. CDAT8 is able to recognize 30 different tRNAs mainly by interacting with the tRNA acceptor stem, including the universal 3'-CCA end, and a flexible base C8
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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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
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Enzyme Nomenclature
3.5.4.35 tRNA(cytosine8) deaminase
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