Target Name: KMT5B
NCBI ID: G51111
Review Report on KMT5B Target / Biomarker Content of Review Report on KMT5B Target / Biomarker
KMT5B
Other Name(s): [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B | Lysine-specific methyltransferase 5B | Lysine N-methyltransferase 5B | OTTHUMP00000197488 | Su(var)4-20 homolog 1 | lysine N-methyltransferase 5B | MGC703 | KMT5B variant 1 | Histone-lysine N-methyltransferase KMT5B (isoform 1) | Suv4-20h1 | Lysine methyltransferase 5B, transcript variant 1 | MGC21161 | CGI85 | MGC118909 | CGI-85 | [histone H4]-lysine20 N-methyltransferase KMT5B | Suppressor of variegation 4-20 homolog 1 | Histone-lysine N-methyltransferase SUV420H1 | OTTHUMP00000197482 | lysine (K)-specific methyltransferase 5B | suppressor of variegation 4-20 homolog 1 | MGC118906 | MRD51 | lysine-specific methyltransferase 5B | su(var)4-20 homolog 1 | lysine methyltransferase 5B | SUV420H1 | C630029K18Rik | histone-lysine N-methyltransferase SUV420H1 | KMT5B_HUMAN | Histone-lysine N-methyltransferase KMT5B

KMT5B: An NMT Enzyme with Potential Applications in Cancer Treatment

Histone modifications are a common modification in eukaryotic cells, which play important roles in various cellular processes. One of the most well-known histone modifications is N-methyltransferase (NMT), an important enzyme involved in regulating staining Quality structure and stability. Among this type of enzyme, KMT5B is an enzyme widely present in various organisms, and its function is to methylate lysine 20 of histones. NMT enzymes play an important role in biological processes such as gene expression, cell cycle, and DNA damage repair. In recent years, studies have found that KMT5B has potential application value in the treatment of certain diseases, and is also considered an important target as a drug target. This article will conduct in-depth research on the discovery, mechanism of action, and drug targets of KMT5B, with a view to providing useful reference for research in related fields.

Discovery and mechanism of action of KMT5B

KMT5B is an NMT enzyme, and its catalytic activity depends on the prosthetic group of NMT enzyme. The prosthetic groups of NMT enzyme mainly include NAD+, FAD and GDP, etc., which play an important auxiliary role in the activity of KMT5B. NAD+ is an important prosthetic group that can reduce the activation energy of KMT5B, thereby improving its catalytic activity. FAD and GDP can also assist the catalytic activity of KMT5B. They can provide the electron pairs required by KMT5B, thereby reducing the activation energy of KMT5B.

The mechanism of action of KMT5B mainly relies on its methylation of histones. Histone is an important protein in chromatin, which is mainly responsible for maintaining the structure and stability of chromatin. Methylation is an important histone modification that can affect the structure, stability and function of histones. KMT5B changes the structure and stability of histones by methylating lysine 20 of histones, thereby affecting the biological processes of chromatin.

The role of KMT5B in tumorigenesis and development

KMT5B plays an important role in tumor occurrence and development. Studies have found that the methylation level of KMT5B is closely related to tumor occurrence and development. For example, methylation levels of KMT5B are positively correlated with breast cancer risk. In addition, the methylation level of KMT5B is also related to tumor invasion and metastasis. These findings indicate that KMT5B has important biological significance in tumor occurrence and development.

Drug targets for KMT5B

As a drug target, KMT5B has important application value in tumor treatment. Currently, there are many studies devoted to finding drugs for KMT5B. For example, KMT5B inhibitors have been used to treat a variety of tumors, such as breast cancer, lung cancer, and prostate cancer. These drugs kill tumor cells by inhibiting the activity of KMT5B, thereby bringing better therapeutic effects to tumor patients.

In addition, some studies are also dedicated to exploring KMT5B as a biomarker for tumors. Studies have found that the methylation level of KMT5B can be used as a biomarker for tumors. Using this, tumors can be diagnosed early, disease prognosis can be assessed, and treatment plans can be formulated.

in conclusion

KMT5B is an important NMT enzyme that plays an important role in biological processes. Its activity depends on the prosthetic groups of NMT enzyme, including NAD+, FAD and GDP. KMT5B changes the structure and stability of histones by methylating lysine 20 of histones, thereby affecting the biological processes of chromatin. In tumor occurrence and development, the methylation level of KMT5B is closely related to the risk, invasion and metastasis of tumors. In addition, the methylation level of KMT5B can also be used as a tumor biomarker, providing an important basis for early diagnosis of tumors, assessment of disease prognosis and formulation of treatment plans. Therefore, KMT5B has important research value as a drug target.

Protein Name: Lysine Methyltransferase 5B

Functions: Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity (PubMed:24396869, PubMed:28114273). In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (PubMed:24396869). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3 (PubMed:23720823). Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (PubMed:28114273). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity)

The "KMT5B Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about KMT5B comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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KMT5C | KNCN | KNDC1 | KNG1 | KNL1 | KNOP1 | KNOP1P5 | KNSTRN | KNTC1 | KPNA1 | KPNA2 | KPNA3 | KPNA4 | KPNA5 | KPNA6 | KPNA7 | KPNB1 | KPNB1-DT | KPRP | KPTN | KRAS | KRASP1 | KRBA1 | KRBA2 | KRBOX1 | KRBOX1-AS1 | KRBOX4 | KRBOX5 | KRCC1 | KREMEN1 | KREMEN2 | KRI1 | KRIT1 | KRR1 | KRT1 | KRT10 | KRT10-AS1 | KRT12 | KRT126P | KRT13 | KRT14 | KRT15 | KRT16 | KRT16P1 | KRT16P2 | KRT16P3 | KRT16P6 | KRT17 | KRT17P1 | KRT17P2 | KRT17P3 | KRT17P5 | KRT17P7 | KRT18 | KRT18P1 | KRT18P12 | KRT18P13 | KRT18P16 | KRT18P17 | KRT18P19 | KRT18P22 | KRT18P23 | KRT18P24 | KRT18P27 | KRT18P28 | KRT18P29 | KRT18P31 | KRT18P33 | KRT18P34 | KRT18P4 | KRT18P40 | KRT18P41 | KRT18P42 | KRT18P44 | KRT18P48 | KRT18P49 | KRT18P5 | KRT18P50 | KRT18P51 | KRT18P55 | KRT18P59 | KRT18P6 | KRT18P62 | KRT19 | KRT19P2 | KRT19P3 | KRT2 | KRT20 | KRT222 | KRT23 | KRT24 | KRT25 | KRT26 | KRT27 | KRT28 | KRT3 | KRT31 | KRT32 | KRT33A | KRT33B