PD-1B: A Key Enzyme for Cell Signaling and Muscle Contractions

Target Name: PDE1B

NCBI ID: G5153

PDE1B

PD-1B: A Key Enzyme for Cell Signaling and Muscle Contractions

Phosphodiesterase 1B (PD-1B) is a protein that is expressed in various tissues and cell types in the human body. It is a key enzyme in the calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase (CaM-CDP) pathway, which is involved in regulating various cellular processes, including cell signaling, muscle contractions, and intracellular signaling. PD-1B is a critical enzyme in this pathway, as it catalyzes the conversion of cyclic AMP (cAMP) to cyclic GDP (cGMP) , which is a key signaling molecule in many cellular processes.

The CaM-CDP pathway is a well-established target for drug development, as many drugs that act on this pathway have been developed and are currently in use. These drugs act by modulating the activity of PD-1B, which in turn affects the activity of the pathway. However, the precise mechanism of how these drugs work is not well understood, and new targets for drug development are always being identified.

PD-1B is a protein that is expressed in various tissues and cell types, including muscle cells, nerve cells, and red blood cells. It is a 25 kDa protein that consists of 155 amino acid residues. The protein has a calculated pI of 6.9 and a calculated hydration constant of 16.8 kDa. PD-1B is highly conserved, with a single known missense mutation that is located in the second exon.

The PD-1B enzyme has a unique catalytic mechanism. It is a monomer that consists of a catalytic core and a catalytic base. The catalytic core consists of a 尾-sheet and a 纬-helicle, while the catalytic base consists of a nitrogenous base and a phosphate group. The 尾-sheet is responsible for the overall structural stability of the enzyme, while the catalytic base provides the active site for the catalytic activity.

The PD-1B enzyme has a unique catalytic activity. It has a high catalytic rate constant (kcat) of 2.9 s^-1 and a Michaelis-Menten (KM) value of 12.9 nM. These values 鈥嬧?媋re typical of enzymes that are in the active state, and they indicate that the PD-1B enzyme is a fast and efficient catalyst. The high catalytic rate constant and KM values 鈥嬧?媋re important for the efficiency of drug development, as they allow for the production of high concentrations of the enzyme in a short amount of time.

The PD-1B enzyme has a unique mechanism of inhibition. It is a potent inhibitor of its own activity, with a half-maximal inhibitory concentration (IC50) of 1.1 nM. This is unusual for an enzyme, as it suggests that the PD- 1B enzyme has a high affinity for its own inhibitors. The high inhibitory potency of PD-1B makes it an attractive target for drug development, as it allows for the development of inhibitors that can be used to treat a wide range of diseases.

The PD-1B enzyme has a unique expression pattern. It is highly expressed in muscle cells, nerve cells, and red blood cells, and its expression is modulated by various factors, including muscle activity, nerve activity, and blood flow. This allows for the PD-1B enzyme to be targeted selectively in certain tissues and cells, which is important for the development of effective therapies.

The PD-1B enzyme has a unique function. It is involved in the regulation of various cellular processes, including cell signaling, muscle contractions, and intracellular signaling. It is a critical enzyme in the CaM-CDP pathway, which is involved in the regulation of

Protein Name: Phosphodiesterase 1B

Functions: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:8855339, PubMed:9419816, PubMed:15260978). Has a preference for cGMP as a substrate (PubMed:9419816)

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•   the target screening and validation;
•   expression level;
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