UROD Human

Uroporphyrinogen Decarboxylase Human Recombinant

UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6157
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
Definition and Classification

Decarboxylases, also known as carboxy-lyases, are enzymes that catalyze the removal of a carboxyl group from organic compounds, releasing carbon dioxide (CO₂). These enzymes are classified under the EC number 4.1.1 and are further categorized based on the substrate they act upon. For example, pyruvate decarboxylase catalyzes the decarboxylation of pyruvate . Other notable examples include aromatic-L-amino-acid decarboxylase, glutamate decarboxylase, and histidine decarboxylase .

Biological Properties

Decarboxylases exhibit diverse biological properties, including specific expression patterns and tissue distribution. For instance, aromatic L-amino acid decarboxylases (AADCs) are ubiquitously found in higher organisms due to their role in synthesizing neurotransmitters and alkaloids . These enzymes are expressed in various tissues, including the brain, liver, and kidneys, and are involved in critical physiological processes .

Biological Functions

The primary biological functions of decarboxylases include the conversion of amino acids into neurotransmitters and other biologically active amines. For example, AADCs convert aromatic L-amino acids into monoamines such as dopamine and serotonin, which serve as major neurotransmitters in animals . Additionally, decarboxylases play a role in immune responses and pathogen recognition by participating in the synthesis of biogenic amines that modulate immune cell activity .

Modes of Action

Decarboxylases interact with other molecules and cells through various mechanisms. These enzymes often require cofactors such as pyridoxal 5’-phosphate (PLP) or pyruvic acid to facilitate the decarboxylation reaction . The binding of these cofactors to the enzyme’s active site enables the stabilization of reaction intermediates and the efficient conversion of substrates into products . Downstream signaling cascades triggered by the products of decarboxylase activity can influence cellular processes such as neurotransmission and metabolic regulation .

Regulatory Mechanisms

The expression and activity of decarboxylases are tightly regulated through multiple mechanisms. Transcriptional regulation involves the control of gene expression by transcription factors that respond to cellular signals . Post-translational modifications, such as phosphorylation and acetylation, can modulate enzyme activity and stability . Additionally, feedback inhibition by the end products of decarboxylase reactions can fine-tune enzyme activity to maintain metabolic homeostasis .

Applications

Decarboxylases have significant applications in biomedical research, diagnostic tools, and therapeutic strategies. In research, these enzymes are used to study metabolic pathways and the synthesis of neurotransmitters . Diagnostic tools leverage decarboxylase activity to detect metabolic disorders and monitor disease progression . Therapeutically, decarboxylase inhibitors are employed to treat conditions such as Parkinson’s disease by modulating neurotransmitter levels .

Role in the Life Cycle

Throughout the life cycle, decarboxylases play crucial roles in development, aging, and disease. During development, these enzymes are involved in the synthesis of neurotransmitters that regulate neural differentiation and growth . In aging, changes in decarboxylase activity can impact cognitive function and metabolic health . In disease, dysregulation of decarboxylase activity is associated with neurological disorders, metabolic syndromes, and immune dysfunction .

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