TRNA pseudouridine55 synthase

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tRNA pseudouridine55 synthase
Identifiers
EC no. 5.4.99.25
CAS no. 430429-15-5
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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NCBI proteins

tRNA pseudouridine55 synthase (EC 5.4.99.25, TruB, aCbf5, Pus4, YNL292w (gene), Psi55 tRNA pseudouridine synthase, tRNA:Psi55-synthase, tRNA pseudouridine 55 synthase, tRNA:pseudouridine-55 synthase, Psi55 synthase, tRNA Psi55 synthase, tRNA:Psi55 synthase, tRNA-uridine55 uracil mutase, Pus10, tRNA-uridine54/55 uracil mutase) is an enzyme with systematic name tRNA-uridine55 uracil mutase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

tRNA uridine55 tRNA pseudouridine55

Pseudouridine synthase TruB from Escherichia coli specifically modifies uridine55 in tRNA molecules.

Related Research Articles

In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

<span class="mw-page-title-main">Pseudouridine</span> Chemical compound

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.

In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA-pseudouridine synthase I is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Phosphoribosylaminoimidazolesuccinocarboxamide synthase</span> Class of enzymes

In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction

TRNA (pseudouridine54-N1)-methyltransferase (EC 2.1.1.257, TrmY, m1Psi methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

Ribonuclease E is a bacterial ribonuclease that participates in the processing of ribosomal RNA and the chemical degradation of bulk cellular RNA.

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 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

tRNA pseudouridine32 synthase is an enzyme with systematic name tRNA-uridine32 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

21S rRNA pseudouridine2819 synthase is an enzyme with systematic name 21S rRNA-uridine2819 uracil mutase. This enzyme catalyses the following chemical reaction

Mitochondrial tRNA pseudouridine27/28 synthase is an enzyme with systematic name mitochondrial tRNA-uridine27/28 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. Nurse K, Wrzesinski J, Bakin A, Lane BG, Ofengand J (March 1995). "Purification, cloning, and properties of the tRNA psi 55 synthase from Escherichia coli". RNA. 1 (1): 102–12. PMC   1369054 . PMID   7489483.
  2. Becker HF, Motorin Y, Planta RJ, Grosjean H (November 1997). "The yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNAs". Nucleic Acids Research. 25 (22): 4493–9. doi:10.1093/nar/25.22.4493. PMC   147073 . PMID   9358157.
  3. Pieńkowska J, Wrzesiński J, Szweykowska-Kulińska Z (1998). "A cell-free yellow lupin extract containing activities of pseudouridine 35 and 55 synthases". Acta Biochimica Polonica. 45 (3): 745–54. doi: 10.18388/abp.1998_4268 . PMID   9918501.
  4. Chaudhuri BN, Chan S, Perry LJ, Yeates TO (June 2004). "Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft". The Journal of Biological Chemistry. 279 (23): 24585–91. doi: 10.1074/jbc.m401045200 . PMID   15028724.
  5. Hoang C, Hamilton CS, Mueller EG, Ferré-D'Amaré AR (August 2005). "Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain". Protein Science. 14 (8): 2201–6. doi:10.1110/ps.051493605. PMC   2279332 . PMID   15987897.
  6. Gurha P, Gupta R (December 2008). "Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in tRNA". RNA. 14 (12): 2521–7. doi:10.1261/rna.1276508. PMC   2590954 . PMID   18952823.