The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: 23S rRNA pseudouridine746 synthase
Reaction: 23S rRNA uridine746 = 23S rRNA pseudouridine746
Other name(s): RluA (ambiguous); 23S RNA PSI746 synthase; 23S rRNA pseudouridine synthase; pseudouridine synthase RluA (ambiguous)
Systematic name: 23S rRNA-uridine746 uracil mutase
Comments: RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine746 [2]. The dual-specificity enzyme also catalyses the formation of uridine32 in tRNA [3]. cf. EC (tRNA pseudouridine32 synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Hoang, C., Chen, J., Vizthum, C.A., Kandel, J.M., Hamilton, C.S., Mueller, E.G. and Ferre-D'Amare, A.R. Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure. Mol. Cell 24 (2006) 535–545. [PMID: 17188032]
2.  Raychaudhuri, S., Niu, L., Conrad, J., Lane, B.G. and Ofengand, J. Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA. J. Biol. Chem. 274 (1999) 18880–18886. [PMID: 10383384]
3.  Wrzesinski, J., Nurse, K., Bakin, A., Lane, B.G. and Ofengand, J. 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 (1995) 437–448. [PMID: 7493321]
[EC created 2011]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald