TRNA dimethylallyltransferase

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TRNA dimethylallyltransferase
Identifiers
EC no. 2.5.1.75
Databases
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BRENDA BRENDA entry
ExPASy NiceZyme view
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MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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NCBI proteins

TRNA dimethylallyltransferase (EC 2.5.1.75, tRNA prenyltransferase, MiaA, transfer ribonucleate isopentenyltransferase, Delta2-isopentenyl pyrophosphate:tRNA-Delta2-isopentenyl transferase, Delta2-isopentenyl pyrophosphate:transfer ribonucleic acid Delta2-isopentenyltransferase) is an enzyme with systematic name dimethylallyl-diphosphate: tRNA dimethylallyltransferase. [1] [2] [3] This enzyme catalyses the following chemical reaction

Contents

dimethylallyl diphosphate + tRNA diphosphate + tRNA containing 6-dimethylallyladenosine

Formerly known as tRNA isopentenyltransferase (EC 2.5.1.8), but it is now known that dimethylallyl diphosphate, rather than isopentenyl diphosphate, is the substrate.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QGN.

Related Research Articles

<span class="mw-page-title-main">Isopentenyl-diphosphate delta isomerase</span> Class of enzymes

Isopentenyl pyrophosphate isomerase, also known as Isopentenyl-diphosphate delta isomerase, is an isomerase that catalyzes the conversion of the relatively un-reactive isopentenyl pyrophosphate (IPP) to the more-reactive electrophile dimethylallyl pyrophosphate (DMAPP). This isomerization is a key step in the biosynthesis of isoprenoids through the mevalonate pathway and the MEP pathway.

In enzymology, a tRNA sulfurtransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Diphosphomevalonate decarboxylase</span> InterPro Family

Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Arginine—tRNA ligase</span>

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

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

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

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

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

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

<span class="mw-page-title-main">Methionine—tRNA ligase</span>

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

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

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

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

In enzymology, an adenylate dimethylallyltransferase (EC 2.5.1.27) is an enzyme that catalyzes the chemical reaction

In enzymology, an aspulvinone dimethylallyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a geranyltranstransferase is an enzyme that catalyzes the chemical reaction

4-Hydroxy-3-methylbut-2-enyl diphosphate reductase (EC 1.17.1.2, isopentenyl-diphosphate:NADP+ oxidoreductase, LytB, (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase, HMBPP reductase, IspH, LytB/IspH) is an enzyme in the non-mevalonate pathway. It acts upon (E)-4-Hydroxy-3-methyl-but-2-enyl pyrophosphate (or "HMB-PP").

<span class="mw-page-title-main">Polyprenyl synthetase</span>

Polyprenyl synthetases are a class of enzymes responsible for synthesis of isoprenoids. Isoprenoid compounds are synthesized by various organisms. For example, in eukaryotes the isoprenoid biosynthetic pathway is responsible for the synthesis of a variety of end products including cholesterol, dolichol, ubiquinone or coenzyme Q. In bacteria this pathway leads to the synthesis of isopentenyl tRNA, isoprenoid quinones, and sugar carrier lipids. Among the enzymes that participate in that pathway, are a number of polyprenyl synthetase enzymes which catalyze a 1'4-condensation between 5-carbon isoprene units. It has been shown that all the above enzymes share some regions of sequence similarity. Two of these regions are rich in aspartic-acid residues and could be involved in the catalytic mechanism and/or the binding of the substrates.

All-trans-nonaprenyl-diphosphate synthase is an enzyme with systematic name geranyl-diphosphate:isopentenyl-diphosphate transtransferase . This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">All-trans-octaprenyl-diphosphate synthase</span> Class of enzymes

All-trans-octaprenyl-diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase . This enzyme catalyses the following chemical reaction

References

  1. ↑ Leung HC, Chen Y, Winkler ME (May 1997). "Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12". The Journal of Biological Chemistry. 272 (20): 13073–83. doi: 10.1074/jbc.272.20.13073 . PMID   9148919.
  2. ↑ Soderberg T, Poulter CD (May 2000). "Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop". Biochemistry. 39 (21): 6546–53. doi:10.1021/bi992775u. PMID   10828971.
  3. ↑ Moore JA, Mathis JR, Poulter CD (June 2000). "Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: pre-steady-state kinetic studies". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1479 (1–2): 166–74. doi:10.1016/S0167-4838(00)00031-5. PMID   11004538.

Literature

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