TRNA pseudouridine65 synthase

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tRNA pseudouridine65 synthase
Identifiers
EC no. 5.4.99.26
CAS no. 430429-15-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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NCBI proteins

tRNA pseudouridine65 synthase (EC 5.4.99.26, TruC, YqcB) is an enzyme with systematic name tRNA-uridine65 uracil mutase. [1] This enzyme catalyses the following chemical reaction

tRNA uridine 65 tRNA pseudouridine65

TruC specifically modifies uridines at positions 65 in tRNA.

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.

<span class="mw-page-title-main">Amino acid synthesis</span> The set of biochemical processes by which amino acids are produced

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).

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

In enzymology, an alanine—tRNA ligase is an enzyme that catalyzes the chemical reaction

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

In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis.

Radical SAM is a designation for a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. rSAMs comprise the largest superfamily of metal-containing enzymes.

TRNA-dihydrouridine20 synthase (NAD(P)+) (EC 1.3.1.91, Dus2p, tRNA-dihydrouridine synthase 2) is an enzyme with systematic name tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase. 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 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 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

tRNA pseudouridine31 synthase is an enzyme with systematic name tRNA-uridine31 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. Del Campo M, Kaya Y, Ofengand J (November 2001). "Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli". RNA. 7 (11): 1603–15. PMC   1370202 . PMID   11720289.