Target Name: OGDH
NCBI ID: G4967
Review Report on OGDH Target / Biomarker Content of Review Report on OGDH Target / Biomarker
OGDH
Other Name(s): Oxoglutarate decarboxylase | OGDC | oxoglutarate dehydrogenase (succinyl-transferring) | testicular tissue protein Li 131 | oxoglutarate decarboxylase | Alpha-ketoglutarate dehydrogenase | OGDHD | Alpha-KGDH-E1 | E1k | oxoglutarate (alpha-ketoglutarate) dehydrogenase (lipoamide) | oxoglutarate dehydrogenase | ODO1_HUMAN | AKGDH | E1o | OGDH-E1 | Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase | 2-oxoglutarate dehydrogenase complex component E1 | alpha-KGDH-E1 | OGDH variant 1 | 2-oxoglutarate dehydrogenase, mitochondrial precursor | Oxoglutarate dehydrogenase (succinyl-transferring) | thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase | KGD1 | Oxoglutarate dehydrogenase, transcript variant 1 | 2-oxoglutarate dehydrogenase, mitochondrial | 2-oxoglutarate dehydrogenase complex component E1 (isoform 1) | OGDC-E1 | OGDH2

OGDH as A Drug Target and Biomarker for Diseases

OGDH (Oxoglutarate decarboxylase) is an enzyme that plays a critical role in the metabolism of the amino acid glutamic acid. Glutamic acid is a key component of protein and is involved in many cellular processes, including signal transduction, muscle contractions, and neurotransmitter synthesis. OGDH is responsible for breaking down glutamic acid to its more essential form, which is then used by other enzymes to synthesize proteins.

The research on OGDH has identified it as a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

OGDH as a drug target
OGDH has been shown to be involved in many cellular processes that are crucial for human health and disease. One of the key functions of OGDH is its role in the regulation of protein synthesis, which is essential for the development and maintenance of tissues and organs. In addition, OGDH is involved in the regulation of cell signaling, which is critical for the proper functioning of tissues and organs.

Studies have shown that OGDH is often mutated in various diseases, including cancer. Mutations in OGDH have been linked to the development of cancer, including breast, ovarian, and colorectal cancers. In addition, OGDH has also been shown to be involved in the development of neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases.

OGDH as a biomarker
OGDH has also been shown to be a potential biomarker for various diseases. For example, OGDH has been shown to be elevated in the brains of individuals with Alzheimer's disease, which is a neurodegenerative disease. In addition, OGDH has also been shown to be elevated in the blood of individuals with Parkinson's disease, which is another neurodegenerative disease.

In addition, OGDH has also been shown to be a potential biomarker for certain autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis. These disorders are characterized by the immune system attacking the body's own tissues, leading to inflammation and pain.

OGDH as a drug target
The research on OGDH has identified it as a potential drug target for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. One of the key strategies for targeting OGDH is to develop small molecules that can inhibit its activity. This can be done by modifying the structure of OGDH to make it less stable or by introducing chemical groups that can interact with its active site.

Another approach for targeting OGDH is to use antibodies that recognize and target specific regions of OGDH. This can be done to either activate or inhibit OGDH's activity, depending on the desired outcome.

In conclusion, OGDH is an enzyme that plays a critical role in the metabolism of glutamic acid and has been identified as a potential drug target or biomarker for various diseases. Further research is needed to fully understand its role in human health and disease.

Protein Name: Oxoglutarate Dehydrogenase

Functions: 2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC (PubMed:24495017, PubMed:25210035, PubMed:28435050). Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids (PubMed:25210035). Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate (PubMed:28435050). Mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711)

The "OGDH 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 OGDH 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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