TRNA pseudouridine32 synthase

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tRNA pseudouridine32 synthase
Identifiers
EC no. 5.4.99.28
CAS no. 430429-15-5
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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.

Related Research Articles

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Pseudouridine is an isomer of the nucleoside uridine in which the uracil is attached via a carbon-carbon instead of a nitrogen-carbon glycosidic bond.

The crotonase family comprises mechanistically diverse proteins that share a conserved trimeric quaternary structure, the core of which consists of 4 turns of a (beta/beta/alpha)n superhelix.

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine967-C5)-methyltransferase (EC 2.1.1.176, rsmB (gene), fmu (gene), 16S rRNA m5C967 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine967-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

Quinolinate synthase (EC 2.5.1.72, NadA, QS, quinolinate synthetase) is an enzyme with systematic name glycerone phosphate:iminosuccinate alkyltransferase (cyclizing). This enzyme catalyses the following chemical reaction

TRNA dimethylallyltransferase is an enzyme with systematic name dimethylallyl-diphosphate: tRNA dimethylallyltransferase. This enzyme catalyses the following chemical reaction

Molybdopterin synthase sulfurtransferase is an enzyme with systematic name persulfurated L-cysteine desulfurase:(molybdopterin-synthase sulfur-carrier protein)-Gly-Gly sulfurtransferase. This enzyme catalyses the following chemical reaction

Cyclic pyranopterin monophosphate synthase is an enzyme with systematic name GTP 8,9-lyase . This enzyme catalyses the following chemical reaction

16S rRNA pseudouridine516 synthase (EC 5.4.99.19, 16S RNA pseudouridine516 synthase, 16S PsiI516 synthase, 16S RNA Psi516 synthase, RNA pseudouridine synthase RsuA, RsuA, 16S RNA pseudouridine 516 synthase) is an enzyme with systematic name 16S rRNA-uridine516 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine2457 synthase is an enzyme with systematic name 23S rRNA-uridine2457 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine2604 synthase is an enzyme with systematic name 23S rRNA-uridine2604 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine2605 synthase is an enzyme with systematic name 23S rRNA-uridine2605 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine1911/1915/1917 synthase (EC 5.4.99.23, RluD, pseudouridine synthase RluD) is an enzyme with systematic name 23S rRNA-uridine1911/1915/1917 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine955/2504/2580 synthase is an enzyme with systematic name 23S rRNA-uridine955/2504/2580 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine55 synthase is an enzyme with systematic name tRNA-uridine55 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine65 synthase is an enzyme with systematic name tRNA-uridine65 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine13 synthase is an enzyme with systematic name tRNA-uridine13 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine746 synthase (EC 5.4.99.29, RluA, 23S RNA PSI746 synthase, 23S rRNA pseudouridine synthase, pseudouridine synthase RluA) is an enzyme with systematic name 23S rRNA-uridine746 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine38/39 synthase is an enzyme with systematic name tRNA-uridine38/39 uracil mutase. This enzyme catalyses the following chemical reaction

References

  1. Hoang C, Chen J, Vizthum CA, Kandel JM, Hamilton CS, Mueller EG, Ferré-D'Amaré AR (November 2006). "Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure". Molecular Cell. 24 (4): 535–45. doi: 10.1016/j.molcel.2006.09.017 . PMID   17188032.
  2. Spedaliere CJ, Hamilton CS, Mueller EG (August 2000). "Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues". Biochemistry. 39 (31): 9459–65. doi:10.1021/bi001079n. PMID   10924141.
  3. Raychaudhuri S, Niu L, Conrad J, Lane BG, Ofengand J (July 1999). "Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA". The Journal of Biological Chemistry. 274 (27): 18880–6. doi: 10.1074/jbc.274.27.18880 . PMID   10383384.
  4. Ramamurthy V, Swann SL, Spedaliere CJ, Mueller EG (October 1999). "Role of cysteine residues in pseudouridine synthases of different families". Biochemistry. 38 (40): 13106–11. doi:10.1021/bi9913911. PMID   10529181.
  5. Wrzesinski J, Nurse K, Bakin A, Lane BG, Ofengand J (June 1995). "A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for psi 746 in 23S RNA is also specific for psi 32 in tRNA(phe)". RNA. 1 (4): 437–48. PMC   1482406 . PMID   7493321.
  6. Behm-Ansmant I, Grosjean H, Massenet S, Motorin Y, Branlant C (December 2004). "Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae" (PDF). The Journal of Biological Chemistry. 279 (51): 52998–3006. doi: 10.1074/jbc.m409581200 . PMID   15466869. S2CID   13197875.