BPHL: Key Enzyme for Biphenyl Metabolism and Cellular Signaling

Target Name: BPHL

NCBI ID: G670

BPHL

BPHL: Key Enzyme for Biphenyl Metabolism and Cellular Signaling

BPHL (Biphenyl hydrolase-related protein) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and liver. It is a key enzyme in the metabolism of biphenyls, which are a type of chemical compound that is commonly found in environmental and human organisms. BPHL is involved in breaking down biphenyls, which is important for maintaining the health and function of the body.

BPHL is a member of the superfamily of proteins that are known as G-proteins. G-proteins are a family of transmembrane proteins that are involved in a wide range of cellular processes, including signaling, intracellular signaling, and cellular signaling pathways. BPHL is a type of G-protein that is characterized by its ability to catalyze the hydrolysis of bromophenylalanine, which is a key metabolite of biphenyls.

BPHL is involved in the metabolism of biphenyls by breaking down the ring-shaped molecule into its component parts. This process is critical for maintaining the health and function of the body, as biphenyls can be toxic and can contribute to the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. By breaking down biphenyls, BPHL helps to remove them from the body and prevent them from causing harm.

BPHL is also involved in the regulation of cellular signaling pathways. G-proteins can act as signaling molecules, transmitting signals from the cell surface to the inside of the cell. BPHL is a critical regulator of these signaling pathways, as it can modulate the activity of other proteins that are involved in cellular signaling. This modulation is important for maintaining the balance and homeostasis of the body, as signals from the cell surface can have a significant impact on the behavior and function of the cell.

BPHL is also involved in the regulation of inflammation. G-proteins can play a role in the regulation of inflammatory responses, as they can modulate the activity of immune cells and promote the production of pro-inflammatory cytokines. BPHL is involved in these processes, as it can affect the activity of immune cells and the production of pro-inflammatory cytokines. This involvement in inflammation regulation is important for maintaining the immune system's response to harmful substances and for protecting the body against disease.

In addition to its role in metabolism and inflammation regulation, BPHL is also involved in the regulation of cell survival. G-proteins can act as stress proteins, helping the cell to survive in the face of stress and damage. BPHL is a critical regulator of cell survival, as it can modulate the activity of other stress proteins that help the cell to survive in the face of stress and damage.

BPHL is also involved in the regulation of protein synthesis. G-proteins can act as enzymes that regulate the production of other proteins, including proteins involved in metabolism and signaling. BPHL is a critical regulator of protein synthesis, as it can affect the activity of these other proteins. This involvement in protein synthesis is important for maintaining the diversity and complexity of the body's proteins, which are essential for the development and function of the body.

In conclusion, BPHL (Biphenyl hydrolase-related protein) is a protein that is involved in a wide range of cellular processes that are important for maintaining the health and function of the body. BPHL is a critical regulator of metabolism, inflammation, cell survival, and protein synthesis. As a result, BPHL is an attractive drug target and a potential biomarker for the development of various diseases.

Protein Name: Biphenyl Hydrolase Like

Functions: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose) (PubMed:15450800, PubMed:21892188, PubMed:23102699, PubMed:23474714, PubMed:33186521, PubMed:34321462, PubMed:34019811). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers (PubMed:23102699, PubMed:23481255). It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated (PubMed:21892188, PubMed:23474714, PubMed:33186521). Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG (PubMed:23102699, PubMed:34019811). Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress (PubMed:24906880). Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond (PubMed:33186521). Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (PubMed:23102699). Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   pharmacochemistry experiments;
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•   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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