The Enzyme Database

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EC 5.4.99.28     
Accepted name: tRNA pseudouridine32 synthase
Reaction: tRNA uridine32 = tRNA pseudouridine32
Other name(s): RluA (ambiguous); pseudouridine synthase RluA (ambiguous); Pus9p; Rib2/Pus8p
Systematic name: tRNA-uridine32 uracil mutase
Comments: The dual-specificity enzyme from Escherichia coli also catalyses the formation of pseudouridine746 in 23S rRNA [5]. cf. EC 5.4.99.29 (23S rRNA pseudouridine746 synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 430429-15-5
References:
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. [DOI] [PMID: 17188032]
2.  Spedaliere, C.J., Hamilton, C.S. and Mueller, E.G. Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues. Biochemistry 39 (2000) 9459–9465. [DOI] [PMID: 10924141]
3.  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. [DOI] [PMID: 10383384]
4.  Ramamurthy, V., Swann, S.L., Spedaliere, C.J. and Mueller, E.G. Role of cysteine residues in pseudouridine synthases of different families. Biochemistry 38 (1999) 13106–13111. [DOI] [PMID: 10529181]
5.  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]
6.  Behm-Ansmant, I., Grosjean, H., Massenet, S., Motorin, Y. and Branlant, C. Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004) 52998–53006. [DOI] [PMID: 15466869]
[EC 5.4.99.28 created 2011, modified 2011]
 
 


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