TRNA pseudouridine32 synthase
TRNA pseudouridine32 synthase (EC 5.4.99.28, RluA, pseudouridine synthase RluA, Pus9p, Rib2/Pus8p) is an enzyme with systematic name tRNA-uridine32 uracil mutase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- tRNA uridine32
tRNA pseudouridine32
The dual enzyme from Escherichia coli also catalyses the formation of pseudouridine746 in 23S rRNA.
References
- ↑ Hoang, C., Chen, J., Vizthum, C.A., Kandel, J.M., Hamilton, C.S., Mueller, E.G. and Ferre-D'Amare, A.R. (2006). "Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure". Mol. Cell 24: 535–545. doi:10.1016/j.molcel.2006.09.017. PMID 17188032.
- ↑ Spedaliere, C.J., Hamilton, C.S. and Mueller, E.G. (2000). "Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues". Biochemistry 39: 9459–9465. doi:10.1021/bi001079n. PMID 10924141.
- ↑ Raychaudhuri, S., Niu, L., Conrad, J., Lane, B.G. and Ofengand, J. (1999). "Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA". J. Biol. Chem. 274: 18880–18886. doi:10.1074/jbc.274.27.18880. PMID 10383384.
- ↑ Ramamurthy, V., Swann, S.L., Spedaliere, C.J. and Mueller, E.G. (1999). "Role of cysteine residues in pseudouridine synthases of different families". Biochemistry 38: 13106–13111. doi:10.1021/bi9913911. PMID 10529181.
- ↑ Wrzesinski, J., Nurse, K., Bakin, A., Lane, B.G. and Ofengand, J. (1995). "A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for Ψ746 in 23S RNA is also specific for Ψ32 in tRNAPhe". RNA 1: 437–448. PMID 7493321.
- ↑ Behm-Ansmant, I., Grosjean, H., Massenet, S., Motorin, Y. and Branlant, C. (2004). "Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae". J. Biol. Chem. 279: 52998–53006. doi:10.1074/jbc.m409581200. PMID 15466869.
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