NDUFA6: A Potential Drug Target and Biomarker for NAD+ Homeostasis

Target Name: NDUFA6

NCBI ID: G4700

NDUFA6

NDUFA6: A Potential Drug Target and Biomarker for NAD+ Homeostasis

NAD+ (nicotinamide adenine dinucleotide) is a crucial coenzyme found in all living cells that plays a vital role in various cellular processes, including energy metabolism, DNA replication, and signaling pathways. NAD+ levels are dynamically regulated to maintain homeostasis, and deviations from these homeostasis can lead to diseases such as diabetes, cancer, and aging. One of the key enzymes involved in NAD+ homeostasis is NDUFA6, which is a subcomplex of the NADH dehydrogenase enzyme (ubiquinone), with a molecular weight of 14 kDa. In this article, we will discuss the potential drug target and biomarker properties of NDUFA6, as well as its role in the regulation of NAD+ homeostasis.

The NADH dehydrogenase enzyme is a key enzyme in the electron transport chain of the cell, responsible for converting NADH, a reducing agent, to NAD+, a oxidizing agent. This conversion process produces ATP, which is the energy currency of the cell. The NADH dehydrogenase enzyme is a member of the superfamily of transition metal-dependent enzymes, which include enzymes involved in various cellular processes, including metabolism, redox reactions, and signaling pathways.

NDUFA6 is a subcomplex of the NADH dehydrogenase enzyme that is characterized by its unique molecular weight of 14 kDa. This subcomplex is composed of three subunits, A, B, and C, which are arranged in a specific spatial structure to form the NADH dehydrogenase complex. The subunit A contains the active site, where the substrate NADH binds to the enzyme. The subunit B contains a Rossmann-fold, which is a structural motif that is commonly found in proteins that are involved in protein-protein interactions. C contains a catalytic site, where the enzyme carries out its catalytic activity.

The NADH dehydrogenase enzyme is involved in the regulation of various cellular processes, including energy metabolism, redox reactions, and signaling pathways. One of the critical roles of the NADH dehydrogenase enzyme is in the regulation of NAD+ homeostasis. NAD+ is an essential coenzyme that plays a vital role in various cellular processes, including energy metabolism, DNA replication, and signaling pathways. NAD+ levels are dynamically regulated to maintain homeostasis, and deviations from these homeostasis can lead to diseases such as diabetes, cancer, and aging.

The NDUFA6 subcomplex of the NADH dehydrogenase enzyme is involved in the regulation of NAD+ homeostasis. NDUFA6 functions as a cofactor for the NAD+-dependent enzyme, nicotinamide riboside nucleotide (NAD+) carboxyltransferase (NAD+-CT), which is involved in the synthesis of NAD+ from NAD+-riboside (NAD+-Rib). NAD+-Rib is a precursor molecule that can be synthesized from various precursors, including NAD+, FAD, and FMN. The NAD+-Rib precursor is then converted to NAD+ by the NAD+-CT enzyme, which is dependent on the availability of NAD+-Rib precursor.

NDUFA6 is also involved in the regulation of NAD+ homeostasis by interacting with the NAD+-dependent enzyme, NAD+-dependent superoxide hydredase (NAD+-OH) subcomplex. NAD+-OH is an enzyme that generates reactive oxygen species (ROS) during the electron transport chain , which can damage cellular components and contribute to various diseases, including aging and cancer. The NAD+-OH sub

Protein Name: NADH:ubiquinone Oxidoreductase Subunit A6

Functions: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly (PubMed:30245030). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

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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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