Target type: molecularfunction
Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 36) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 36). This reaction is the addition of a methyl group to the lysine residue at position 36 of the histone H3 protein. [GOC:ai]
Histone H3K36 methyltransferase activity is a molecular function that describes the enzymatic ability to transfer methyl groups from a donor molecule, such as S-adenosyl methionine (SAM), to the lysine residue at position 36 of histone H3. This modification, known as histone H3 lysine 36 methylation (H3K36me), is a crucial epigenetic mark that plays a significant role in regulating gene expression and maintaining genomic integrity.
H3K36 methylation is typically associated with actively transcribed regions of the genome. This modification serves as a signal for the recruitment of various protein complexes that promote transcription elongation, prevent aberrant transcription initiation, and facilitate the accurate processing of pre-mRNA.
The specific molecular function of histone H3K36 methyltransferase activity can be further dissected into the following steps:
1. **Substrate Recognition:** The enzyme recognizes and binds to the histone H3 tail, specifically targeting the lysine 36 residue.
2. **SAM Binding:** The enzyme binds to the methyl donor, SAM, which provides the methyl group for the modification.
3. **Catalysis:** The enzyme catalyzes the transfer of a methyl group from SAM to the lysine 36 residue of histone H3.
4. **Product Release:** The modified histone H3 and the demethylated SAM are released from the enzyme.
The H3K36 methyltransferase activity is carried out by a family of enzymes known as SET domain containing proteins. These enzymes possess a conserved SET domain that is responsible for the catalytic activity.
In summary, histone H3K36 methyltransferase activity is a key regulatory mechanism in gene expression, ensuring accurate transcription and maintaining genomic stability. Its precise molecular function involves the recognition of histone H3, binding of SAM, catalytic transfer of a methyl group, and release of the modified histone H3 and the demethylated SAM.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| N-lysine methyltransferase SMYD2 | An N-lysine methyltransferase SMYD2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NRG4] | Homo sapiens (human) |
| Histone-lysine N-methyltransferase SETMAR | A histone-lysine N-methyltransferase SETMAR that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q53H47] | Homo sapiens (human) |
| Histone-lysine N-methyltransferase NSD2 | A histone-lysine N-methyltransferase NSD2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O96028] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| s-adenosylhomocysteine | S-adenosyl-L-homocysteine : An organic sulfide that is the S-adenosyl derivative of L-homocysteine. S-Adenosylhomocysteine: 5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions. | adenosines; amino acid zwitterion; homocysteine derivative; homocysteines; organic sulfide | cofactor; EC 2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)] inhibitor; EC 2.1.1.79 (cyclopropane-fatty-acyl-phospholipid synthase) inhibitor; epitope; fundamental metabolite |
| scutellarein | scutellarein : Flavone substituted with hydroxy groups at C-4', -5, -6 and -7. scutellarein: aglycone of scutellarin from Scutellaria baicalensis; carthamidin is 2S isomer of scutellarein; do not confuse with isoscutellarein and/or isocarthamidin which are respective regioisomers, or with the scutelarin protein | tetrahydroxyflavone | metabolite |
| az 505 | AZ 505: an SMYD2 inhibitor; structure in first source | ||
| gsk343 | GSK343 : A member of the class of indazoles that is 1-isopropyl-1H-indazole-4-carboxamide in which the nitrogen of the carboxamide group is substituted by a (6-methyl-2-oxo-4-propyl-1,2-dihydropyridin-3-yl)methyl group and in which the indazole ring is substituted at position 6 by a 2-(4-methylpiperazin-1-yl)pyridin-4-yl group. A highly potent and selective EZH2 inhibitor (IC50 = 4 nM). GSK343: an EZH2 methyltransferase inhibitor | aminopyridine; indazoles; N-alkylpiperazine; N-arylpiperazine; pyridone; secondary carboxamide | antineoplastic agent; apoptosis inducer; EC 2.1.1.43 (enhancer of zeste homolog 2) inhibitor |
| 6,7-dimethoxy-2-(pyrrolidin-1-yl)-n-(5-(pyrrolidin-1-yl)pentyl)quinazolin-4-amine | 6,7-dimethoxy-2-(pyrrolidin-1-yl)-N-(5-(pyrrolidin-1-yl)pentyl)quinazolin-4-amine: a SETD8 inhibitor; structure in first source | ||
| lly-507 | LLY-507 : A secondary carboxamide resulting from the formal condensation of the carboxy group of 5-cyano-2'-{4-[2-(3-methyl-1H-indol-1-yl)ethyl]piperazin-1-yl}[biphenyl]-3-carboxylic acid with the amino group of 3-(pyrrolidin-1-yl)propan-1-amine. It is a potent and selective inhibitor of SMYD2 and inhibits the ability of SMYD2 to methylate p53. It serves as a valuable chemical probe to aid in the dissection of SMYD2 function in cancer and other biological processes. LLY-507: inhibits methyltransferase SMYD2; structure in first source |