• Mycobiology
• /
• v.47 no.4
• /
• pp.441-448
• /
• 2019

Two new SAM-dependent methyltransferase encoding genes (fvsmt1 and fvsmt2) were identified from the genome of Flammulina velutipes. In order to make a comprehensive characterization of both genes, we performed in silico analysis of both genes and used qRT-PCR to reveal their expression patterns during the development of F. velutipes. There are 4 and 6 exons with total length of 693 and 978 bp in fvsmt2 and fvsmt1, respectively. The deduced proteins, i.e., FVSMT1 and FVSMT2 contained 325 and 230 amino acids with molecular weight 36297 and 24894 Da, respectively. Both proteins contained a SAM-dependent catalytic domain with signature motifs (I, p-I, II, and III) defining the SAM fold. SAM-dependent catalytic domain is located either in the middle or at the N-terminal of FVSMT2 and FVSMT1, respectively. Alignment and phylogenic analysis showed that FVSMT1 is a homolog to a protein-arginine omega-N-methyltransferase, while FVSMT2 is of cinnamoyl CoA O-methyltransferase type and predicted subcellular locations of these proteins are mitochondria and cytoplasm, respectively. qRT-PCR showed that fvsmt1 and fvsmt2 expression was regulated in different developmental stages. The maximum expression levels of fvsmt1 and fvsmt2 were observed in stipe elongation, while no difference was found in mycelium and pileus. These results positively demonstrate that both the methyltransferase encoding genes are involved in the stipe elongation of F. velutipes.

• Korean Journal of Biological Psychiatry
• /
• v.8 no.1
• /
• pp.111-115
• /
• 2001

An association study with Korean alcoholic patients(n=50) and normal controls(n=53) was performed to find the relationship between catechol-O-methyltransferase(COMT) gene polymorphism and alcoholism using polymerase chain reaction-restriction fragment length polymorphism. When we compared the allele and genotype frequencies of Nla III COMT gene polymorphism in alcoholism and normal controls, there was no significant difference between two groups. Our results do not support an association between the Nla III polymorphism of COMT gene and alcoholism.

• Bulletin of the Korean Chemical Society
• /
• v.30 no.11
• /
• pp.2803-2805
• /
• 2009

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.979-979
• /
• 2005

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.982-982
• /
• 2005

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.1003-1003
• /
• 2005

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.1006-1006
• /
• 2005

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.978-978
• /
• 2005

• Bulletin of the Korean Chemical Society
• /
• v.24 no.9
• /
• pp.1256-1260
• /
• 2003

Two O-methyltransferases, OMTII-1 and OMTII-4 of meadow rue Thalictrum tuberosum showed a high sequence identity. Of 364 amino acids only one residue is not the same, which is Tyr21 or Cys21. Even if the 21st residues in these OMTs are not included in the binding sites of the enzymes, binding affinities of the enzyme homodimers over the same substrate are very different. While the binding affinity of one homodimer over caffeic acid is 100%, that of the other is 25%. Authors tried to predict the three-dimensional structures of Thalictrum tuberosum O-methyltransferases using homology-based modelling by a comparison with caffeic acid O-methyltransferase, and explain the reason of the phenomenon mentioned above based on their three dimensional structural studies. In the enzyme homodimer, the better binding affinity may be caused by the shorter distance between the 21st residue and the binding site of the other monomer.

• BMB Reports
• /
• v.32 no.3
• /
• pp.299-305
• /
• 1999

Protein carboxyl O-methyltransferase (PCMT) catalyzes the transfer of a methyl group from Sadenosyl-L-methionine to free carboxyl groups of methyl-accepting substrate proteins. Two isozymes were separated by DEAE-Sephacel chromatography from porcine brain cytosol and designated PCMT I and II. Isozymes I and II were further purified by adenosyl homocysteine-Sepharose 4B and Superose HR 12 chromatography. The molecular weights of the purified PCMT I and II were determined by mass spectrometry to be 20,138 Da and 25,574 Da, respectively. The two enzymes displayed different isoelectric points; 7.9 for PCMT I and 5.3 for PCMT II. Isozymes I and II exhibited similar substrate specificities when tested with various methyl-accepting proteins. Myelin basic protein, a component of myelinated neurons, was found to be an excellent methyl-accepting substrate for both PCMT isozymes with different $K_m$ values, $21.1\;{\mu}M$ for PCMT I and $10.6\;{\mu}M$ for PCMT II. The PCMT activity and methyl-accepting capacity displayed similar distribution in the various brain regions with an exception of the lower values in the cerebellum. The overall distribution may relate to a general function of protein repair by PCMT in the brain.