Target Name: FDFT1
NCBI ID: G2222
Review Report on FDFT1 Target / Biomarker Content of Review Report on FDFT1 Target / Biomarker
FDFT1
Other Name(s): Farnesyl-diphosphate farnesyltransferase 1, transcript variant 9 | Farnesyl-diphosphate farnesyltransferase 1 | FDFT1 variant 3 | squalene synthase | Farnesyl-diphosphate farnesyltransferase 1, transcript variant 4 | squalene synthetase | FDFT1 variant 2 | Farnesyl-diphosphate farnesyltransferase | Presqualene synthase | ERG9 | Farnesyl-diphosphate farnesyltransferase 1, transcript variant 1 | Presqualene-di-diphosphate synthase | SQSD | Presqualene-diphosphate synthase | presqualene-di-diphosphate synthase | FDFT1 variant 4 | Squalene synthetase | Squalene synthase (isoform 3) | farnesyl-diphosphate farnesyltransferase 1 | Squalene synthase (isoform 1) | FDFT1 variant 9 | Farnesyl-diphosphate farnesyltransferase 1, transcript variant 2 | FDFT1 variant 1 | FDFT_HUMAN | FPP:FPP farnesyltransferase | DGPT | Farnesyl-diphosphate farnesyltransferase 1, transcript variant 3 | SS | Squalene synthase | SQS | Squalene synthase (isoform 2) | Farnesyltransferase

FDFT1: A Protein Involved in Farnesyl Transfer and Potential Drug Target

FDFT1, also known as Farnesyl-diphosphate farnesyltransferase 1, is a protein that plays a crucial role in the transfer of phosphate groups from the substrate to theacylhydrazine (Ash) side chain of the transmembrane protein Farnesylated proteins. This enzyme is composed of 254 amino acids and has a molecular weight of 31 kDa. It is a member of the superfamily of transferases, which includes enzymes that transfer phosphate or other groups from one molecule to another.

FDFT1 is expressed in a variety of tissues and cells, including the heart, brain, and peripheral tissues. It is also highly expressed in the testes, which suggests that it may be involved in male reproductive function. In addition, it is expressed in the liver, which is known as the primary site of farnesylation in the body.

FDFT1 has been shown to play a role in the regulation of various cellular processes, including cell growth, differentiation, and metabolism. It has been shown to promote the growth and survival of cancer cells, and it has also been shown to play a role in the regulation of the immune response.

FDFT1 has also been shown to be a potential drug target. The ability of this enzyme to transfer phosphate groups from its substrate to theacylhydrazine (Ash) side chain of other proteins makes it a potential target for small molecules that can inhibit its activity. This has led to the development of a new class of drugs called inhibitors of FDFT1, which are being studied for their potential use in treating a variety of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.

In addition to its potential as a drug target, FDFT1 has also been shown to be a valuable biomarker for certain diseases. The levels of FDFT1 have been shown to be elevated in a variety of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. This suggests that FDFT1 may be a useful diagnostic or therapeutic target in these diseases.

Overall, FDFT1 is a highly conserved protein that plays a critical role in the regulation of various cellular processes. Its potential as a drug target and biomarker makes it an attractive target for the development of new therapies for a variety of diseases. Further research is needed to fully understand the role of FDFT1 in the regulation of cellular processes and its potential as a drug target.

Protein Name: Farnesyl-diphosphate Farnesyltransferase 1

Functions: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. Proceeds in two distinct steps. In the first half-reaction, two molecules of FPP react to form the stable presqualene diphosphate intermediate (PSQPP), with concomitant release of a proton and a molecule of inorganic diphosphate. In the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with NADPH or NADH to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway

The "FDFT1 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 FDFT1 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

More Common Targets

FDPS | FDPSP2 | FDPSP4 | FDPSP5 | FDPSP6 | FDPSP7 | FDX1 | FDX2 | FDXACB1 | FDXR | FECH | FEM1A | FEM1AP4 | FEM1B | FEM1C | FEN1 | FENDRR | FER | FER1L4 | FER1L5 | FER1L6 | FER1L6-AS1 | FER1L6-AS2 | FERD3L | FERMT1 | FERMT2 | FERMT3 | Ferritin | FES | Fetal Hemoglobin (HbF) | FETUB | FEV | FEZ1 | FEZ2 | FEZF1 | FEZF1-AS1 | FEZF2 | FFAR1 | FFAR2 | FFAR3 | FFAR4 | FGA | FGB | FGD1 | FGD2 | FGD3 | FGD4 | FGD5 | FGD5-AS1 | FGD5P1 | FGD6 | FGF1 | FGF10 | FGF10-AS1 | FGF11 | FGF12 | FGF12-AS2 | FGF13 | FGF13-AS1 | FGF14 | FGF14-AS1 | FGF14-AS2 | FGF14-IT1 | FGF16 | FGF17 | FGF18 | FGF19 | FGF2 | FGF20 | FGF21 | FGF22 | FGF23 | FGF3 | FGF4 | FGF5 | FGF6 | FGF7 | FGF7P3 | FGF7P5 | FGF7P6 | FGF8 | FGF9 | FGFBP1 | FGFBP2 | FGFBP3 | FGFR1 | FGFR1OP2 | FGFR2 | FGFR3 | FGFR3P1 | FGFR4 | FGFRL1 | FGG | FGGY | FGL1 | FGL2 | FGR | FH | FHAD1 | FHDC1