TRNA (guanine37-N1)-methyltransferase

Last updated
tRNA (guanine37-N1)-methyltransferase
Identifiers
EC no. 2.1.1.228
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

tRNA (guanine37-N1)-methyltransferase (EC 2.1.1.228, TrmD, tRNA (m1G37) methyltransferase, transfer RNA (m1G37) methyltransferase, Trm5p, TRMT5, tRNA-(N1G37) methyltransferase, MJ0883 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine37-N1)-methyltransferase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + guanine 37 in tRNA S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA

This enzyme is important for the maintenance of the correct reading frame during translation.

Related Research Articles

<span class="mw-page-title-main">Methyltransferase</span> Group of methylating enzymes

Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.

mRNA (guanine-N7-)-methyltransferase Enzyme

In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (guanine-N1-)-methyltransferase (EC 2.1.1.51) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (adenine-N1-)-methyltransferase (EC 2.1.1.36) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (guanine-N1-)-methyltransferase (EC 2.1.1.31) is an enzyme that catalyzes the chemical reaction

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

Methyl halide transferase is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase. This enzyme catalyses the following chemical reaction

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 (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine745-N1)-methyltransferase (EC 2.1.1.187, Rlma(I), Rlma1, 23S rRNA m1G745 methyltransferase, YebH, RlmAI methyltransferase, ribosomal RNA(m1G)-methylase, rRNA(m1G)methylase, RrmA, 23S rRNA:m1G745 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine745-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (cytidine32/uridine32-2'-O)-methyltransferase (EC 2.1.1.200, YfhQ, tRNA:Cm32/Um32 methyltransferase, TrMet(Xm32), TrmJ) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine32/uridine32-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (cytidine34-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine2535-N1)-methyltransferase (EC 2.1.1.209, AviRa) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2535-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213, PAB1283, N(2),N(2)-dimethylguanosine tRNA methyltransferase, Trm-G10, PabTrm-G10, PabTrm-m2 2G10 enzyme) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine10-N2)-dimethyltransferase. This enzyme catalyses the following chemical reaction

TRNA (adenine22-N1)-methyltransferase (EC 2.1.1.217, TrmK, YqfN, Sp1610 (gene), tRNA: m1A22 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine22-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (adenine9-N1)-methyltransferase (EC 2.1.1.218, Trm10p, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase, TK0422p (gene), tRNA m1A9-methyltransferase, tRNA m1A9 Mtase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine9-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (adenine57-N1/adenine58-N1)-methyltransferase (EC 2.1.1.219, TrmI, PabTrmI, AqTrmI, MtTrmI) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine57/adenine58-N1)-methyltransferase. This enzyme catalyses the following chemical reaction:

TRNA (adenine58-N1)-methyltransferase (EC 2.1.1.220, tRNA m1A58 methyltransferase, tRNA (m1A58) methyltransferase, TrmI, tRNA (m1A58) Mtase, Rv2118cp, Gcd10p-Gcd14p, Trm61p-Trm6p) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine58-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (guanine9-N1)-methyltransferase (EC 2.1.1.221, Trm10p, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase, tRNA (guanine-N(1)-)-methyltransferase, tRNA m1G9-methyltransferase, tRNA m1G9 MTase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine9-N1)-methyltransferase. This enzyme catalyses the following 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

References

  1. ↑ Takeda H, Toyooka T, Ikeuchi Y, Yokobori S, Okadome K, Takano F, Oshima T, Suzuki T, Endo Y, Hori H (December 2006). "The substrate specificity of tRNA (m1G37) methyltransferase (TrmD) from Aquifex aeolicus". Genes to Cells. 11 (12): 1353–65. doi:10.1111/j.1365-2443.2006.01022.x. PMID   17121543.
  2. ↑ Lee C, Kramer G, Graham DE, Appling DR (September 2007). "Yeast mitochondrial initiator tRNA is methylated at guanosine 37 by the Trm5-encoded tRNA (guanine-N1-)-methyltransferase". The Journal of Biological Chemistry. 282 (38): 27744–53. doi: 10.1074/jbc.m704572200 . PMID   17652090.
  3. ↑ O'Dwyer K, Watts JM, Biswas S, Ambrad J, Barber M, Brulé H, Petit C, Holmes DJ, Zalacain M, Holmes WM (April 2004). "Characterization of Streptococcus pneumoniae TrmD, a tRNA methyltransferase essential for growth". Journal of Bacteriology. 186 (8): 2346–54. doi:10.1128/jb.186.8.2346-2354.2004. PMC   412112 . PMID   15060037.
  4. ↑ Brulé H, Elliott M, Redlak M, Zehner ZE, Holmes WM (July 2004). "Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein". Biochemistry. 43 (28): 9243–55. doi:10.1021/bi049671q. PMID   15248782.
  5. ↑ Goto-Ito S, Ito T, Ishii R, Muto Y, Bessho Y, Yokoyama S (September 2008). "Crystal structure of archaeal tRNA(m(1)G37)methyltransferase aTrm5". Proteins. 72 (4): 1274–89. doi:10.1002/prot.22019. PMID   18384044.
  6. ↑ Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK (June 2003). "Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition". The EMBO Journal. 22 (11): 2593–603. doi:10.1093/emboj/cdg269. PMC   156765 . PMID   12773376.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.