PMPCA: A Zinc-Binding Protease Alpha (G23203)

Target Name: PMPCA

NCBI ID: G23203

PMPCA

PMPCA: A Zinc-Binding Protease Alpha

PMPCA (Protease-Moldersin-Protein-Catalytic alpha), also known as inactive zinc metalloprotease alpha, is a protein that is expressed in various cell types of the human body. It is a member of the metal-dependent proteases (MDP) family, which includes other well-known proteins such as AIMP (Active-inactive Zinc Metalloprotease alpha) and ZAP (Zinc-Accelerated Proteasome-212).

PMPCA is characterized by its unique structure and mechanism of action. It is a 14 kDa protein that consists of a 156 amino acid residue with a calculated pI of 9.6. The protein has a distinct N-terminal region that contains a conserved zinc ion binding site, which is crucial for its catalytic activity.

PMPCA functions as a protease, which means it can break down other proteins into smaller peptides. It is also known as a zinc metalloprotease alpha, which means it uses zinc ions as a cofactor to catalyze the breakdown of other proteins.

PMPCA has been shown to play a crucial role in various cellular processes, including cell signaling, inflammation, and tissue repair. For example, PMPCA has been shown to be involved in the regulation of cell apoptosis, which is the process by which cells decide when to die and are removed from the body.

PMPCA has also been shown to play a role in the regulation of inflammation and fibrosis. For example, studies have shown that PMPCA can inhibit the activity of immune cells and reduce the production of pro-inflammatory cytokines.

PMPCA has also been shown to be involved in the regulation of cell signaling, particularly in the regulation of cell proliferation. For example, studies have shown that PMPCA can inhibit the activity of signaling pathways that are involved in cell proliferation, such as the PI3K/Akt signaling pathway.

PMPCA has a unique mechanism of action that allows it to function as a zinc metalloprotease alpha. It uses zinc ions as a cofactor to activate the proteasome, which is a complex protein that is involved in the breakdown of other proteins. The zinc ions bound to specific sites on the proteasome, which allows PMPCA to catalyze the breakdown of other proteins.

PMPCA has been shown to be involved in the regulation of various cellular processes, including cell signaling, inflammation, and tissue repair. It has also been shown to play a role in the regulation of cell apoptosis, the process by which cells decide when to die and are removed from the body.

In conclusion, PMPCA is a unique protein that is expressed in various cell types of the human body. It is a member of the metal-dependent proteases (MDP) family and has a distinct N-terminal region that contains a conserved zinc ion binding site. PMPCA functions as a zinc metalloprotease alpha and is involved in various cellular processes, including cell signaling, inflammation, and tissue repair. Its unique mechanism of action, as a zinc metalloprotease alpha, makes it a potential drug target or biomarker. Further research is needed to fully understand the role of PMPCA in various cellular processes and to explore its potential as a drug or biomarker.

Protein Name: Peptidase, Mitochondrial Processing Subunit Alpha

Functions: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins

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•   general information;
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•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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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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