Target Name: ALG8
NCBI ID: G79053
Review Report on ALG8 Target / Biomarker Content of Review Report on ALG8 Target / Biomarker
ALG8
Other Name(s): Dolichyl-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichol alpha- 1->3-glucosyltransferase | asparagine-linked glycosylation protein 8 homolog | ALG8 alpha-1,3-glucosyltransferase, transcript variant 1 | ALG8 alpha-1,3-glucosyltransferase, transcript variant 2 | dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase | Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase | Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase | Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase | asparagine-linked glycosylation 8 homolog (yeast, alpha-1,3-glucosyltransferase) | dolichyl-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichol alpha- 1->3-glucosyltransferase | dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl-alpha-1,3-glucosyltransferase | asparagine-linked glycosylation 8 alpha-13-glucosyltransferase-like protein | Asparagine-linked glycosylation 8, alpha-1,3-glucosyltransferase homolog | dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase | HUSSY-02 | Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase | Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (isoform b) | Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (isoform a) | MGC2840 | Asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase) | asparagine-linked glycosylation 8, alpha-1,3-glucosyltransferase homolog | ALG8 alpha-1,3-glucosyltransferase | Dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl-alpha-1,3-glucosyltransferase | asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase) | dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase | CDG1H | ALG8_HUMAN | Asparagine-linked glycosylation 8 homolog (yeast, alpha-1,3-glucosyltransferase) | Asparagine-linked glycosylation 8 alpha-13-glucosyltransferase-like protein | PCLD3 | ALG8 variant 1 | Asparagine-linked glycosylation protein 8 homolog | ALG8 variant 2 | Asparagine-linked glycosylation protein 8

ALG8: Enzyme Involved in Carbohydrate Metabolism and Potential Drug Target

ALG8, or alpha-1->3-glucosyltransferase, is a enzyme involved in the metabolism of dietary carbohydrates to glucose. This enzyme is found in various organisms, including bacteria, archaea, and eukaryotes. It is a critical enzyme in the glycolytic pathway, which is the primary pathway for the metabolism of glucose in eukaryotes.

ALG8 is a transmembrane protein that is located at the end of the longest sub-cellular organelles called mitochondrial mitofusiformes. It has a calculated molecular weight of 170 kDa and a pre-functional activity of 7.9 kDa. The protein has a highly conserved catalytic core, with a catalytic cycle of 215 amino acids residues, which is primarily located in the N-terminal region of the protein.

The primary function of ALG8 is to transfer alpha-1, 4-glucosidic bonds from the 2,3-beta-glucoside to the alpha-1, 3-glucosidic bond. This transfer reaction occurs through a three-step mechanism, which involves the formation of a carbocation intermediate, the transfer of the alpha-1, 4-glucosidic bond to the alpha-1, 3-glucosidic bond, and the formation of a stable alpha-1, 4-glucosidic bond.

ALG8 is a key enzyme in the glycolytic pathway, as it initiates the transfer of the alpha-1, 4-glucosidic bond to the alpha-1, 3-glucosidic bond. This transfer reaction is critical for the efficient metabolism of carbohydrates to glucose, as it allows for the rapid and efficient breakdown of complex carbohydrates into simpler sugars.

In addition to its role in the glycolytic pathway, ALG8 has been shown to have various other functions. For example, it has been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and inflammation. It has also been shown to be involved in the development and progression of various diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases.

Due to its involvement in the metabolism of carbohydrates and its potential role in the regulation of various cellular processes, ALG8 has been identified as a potential drug target or biomarker. Many studies have shown that inhibiting the activity of ALG8 has the potential to treat various diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases.

In conclusion, ALG8 is an important enzyme involved in the metabolism of carbohydrates to glucose. Its function as a key enzyme in the glycolytic pathway and its potential as a drug target or biomarker make it an attractive target for the development of new treatments for various diseases. Further research is needed to fully understand the role of ALG8 in the metabolism of carbohydrates and its potential as a drug.

Protein Name: ALG8 Alpha-1,3-glucosyltransferase

Functions: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol before it is transferred to the nascent peptide (By similarity). Required for PKD1/Polycystin-1 maturation and localization to the plasma membrane of the primary cilia (By similarity)

The "ALG8 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 ALG8 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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