CYP1B1: A Key Enzyme in Energy Production (G1545)

Target Name: CYP1B1

NCBI ID: G1545

CYP1B1: A Key Enzyme in Energy Production

CYP1B1, also known as microsomal monooxygenase, is a enzyme located in the mitochondria that plays a crucial role in the production of energy in the body. It is a key enzyme in the citric acid cycle, which is the process by which the body produces energy from the food we eat.

CYP1B1 is a monooxygenase, which means it produces reactive oxygen species (ROS) as a byproduct of its catalytic activity. These ROS can damage cellular components and contribute to a variety of diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases.

One of the unique features of CYP1B1 is its location in the mitochondria. Mitochondria are organelles that are responsible for generating the energy the body needs to function, and they are found in most eukaryotic cells. As a result, CYP1B1 is involved in the production of the energy the body needs to power its many cellular processes.

CYP1B1 is a key enzyme in the citric acid cycle, which is the central metabolic pathway that generates the majority of the energy the body needs to function. The citric acid cycle involves the breakdown of glucose into pyruvate, which is then converted into acetyl-CoA, citrate, and carbon dioxide. This process produces a large amount of ATP, which is the energy currency of the body, as well as a variety of other molecules that are used by the cell.

CYP1B1 is a critical enzyme in the citric acid cycle, and its activity is required for the production of ATP and the production of carbon dioxide. It is also involved in the production of other molecules that are used by the cell, includingNADH, FADH2, and succinyl-CoA.

CYP1B1 is a drug target, and a number of studies have identified it as a potential therapeutic target for a variety of diseases. For example, CYP1B1 has been identified as a potential therapeutic target for cancer, neurodegenerative diseases, and cardiovascular diseases.

One of the reasons why CYP1B1 is a promising drug target is that it is involved in the production of a large number of molecules that are used by the cell. This makes it difficult to target the enzyme and disrupt its activity. Additionally, CYP1B1 is located in the mitochondria, which are known for their stability and resistance to many therapeutic approaches. This makes it difficult to target the enzyme and disrupt its activity.

In addition to its potential as a drug target, CYP1B1 is also a potential biomarker for a variety of diseases. For example, changes in the level of CYP1B1 activity have been identified as a potential biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and cardiovascular diseases.

Overall, CYP1B1 is a unique and important enzyme that plays a critical role in the production of energy in the body. Its location in the mitochondria and its involvement in the production of a large number of molecules make it a promising target for therapeutic intervention. Additionally, its potential as a biomarker for a variety of diseases makes it an important tool for the diagnosis and treatment of these diseases.

Protein Name: Cytochrome P450 Family 1 Subfamily B Member 1

Functions: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position (PubMed:11555828, PubMed:12865317). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (PubMed:10426814). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376, PubMed:15258110). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (PubMed:21068195). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (PubMed:10426814). Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity)

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