Enzymes
Product List
ALAD Human
Aminolevulinate Dehydratase Human Recombinant
ALAD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
AUH Human
AU RNA Binding Protein/Enoyl-CoA Hydratase Human Recombinant
ECH1 Human
Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant
ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ECHDC1 Human
Enoyl CoA Hydratase Domain Containing 1 Human Recombinant
SNAP25 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
ECHS1 Human
Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant
ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ECHS1 Human, Active
Enoyl CoA Hydratase, Short chain, 1, Mitochondrial, Human Recombinant, Active
ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a) and having a molecular mass of 30.6kDa. ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Fumarase Human
Fumarate Hydratase Human Recombinant
Fumarate Hydratase is purified by proprietary chromatographic techniques.
GMDS Human
GDP-Mannose 4,6-Dehydratase Human Recombinant
GMDS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HADHB Human
2-Enoyl-Coenzyme A (CoA) Hydratase, Beta Human Recombinant
PCBD1 Human
Pterin-4-Alpha-Carbinolamine Dehydratase Human Recombinant
PCBD1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Hydratases are enzymes that catalyze the addition or removal of water molecules to or from substrates. They belong to the lyase family, specifically the hydro-lyases, which facilitate the cleavage of carbon-oxygen bonds by means other than hydrolysis or oxidation. Hydratases are classified based on their substrate specificity and the type of reaction they catalyze, such as fumarase, enoyl-CoA hydratase, and aconitase.
Key Biological Properties: Hydratases are crucial for various metabolic pathways, including the citric acid cycle and fatty acid metabolism. They exhibit high substrate specificity and catalytic efficiency.
Expression Patterns: The expression of hydratases varies across different tissues and developmental stages. For instance, fumarase is highly expressed in the liver and kidneys, while enoyl-CoA hydratase is predominantly found in muscle tissues.
Tissue Distribution: Hydratases are ubiquitously distributed in both prokaryotic and eukaryotic organisms. They are present in various cellular compartments, including the cytoplasm, mitochondria, and peroxisomes.
Primary Biological Functions: Hydratases play a pivotal role in metabolic processes. For example, fumarase catalyzes the reversible hydration of fumarate to malate in the citric acid cycle, while enoyl-CoA hydratase is involved in the β-oxidation of fatty acids.
Role in Immune Responses and Pathogen Recognition: Hydratases contribute to immune responses by modulating metabolic pathways that influence immune cell function. For instance, aconitase activity affects the production of reactive oxygen species, which are crucial for pathogen elimination.
Mechanisms with Other Molecules and Cells: Hydratases interact with various substrates and cofactors to facilitate their catalytic activity. For example, aconitase requires an iron-sulfur cluster for its enzymatic function.
Binding Partners: Hydratases often form complexes with other enzymes or proteins to enhance their stability and activity. For instance, fumarase associates with other enzymes in the citric acid cycle to form a metabolon.
Downstream Signaling Cascades: The activity of hydratases can influence downstream signaling pathways. For example, the products of hydratase-catalyzed reactions can serve as signaling molecules that regulate cellular processes such as apoptosis and proliferation.
Transcriptional Regulation: The expression of hydratases is regulated at the transcriptional level by various transcription factors and signaling pathways. For instance, hypoxia-inducible factors can upregulate the expression of fumarase under low oxygen conditions.
Post-Translational Modifications: Hydratases undergo various post-translational modifications, such as phosphorylation and acetylation, which can modulate their activity, stability, and subcellular localization.
Biomedical Research: Hydratases are used as model enzymes to study metabolic pathways and enzyme kinetics. They also serve as targets for drug development in metabolic disorders and cancer.
Diagnostic Tools: The activity levels of certain hydratases can serve as biomarkers for diseases. For example, decreased fumarase activity is associated with fumarase deficiency, a rare metabolic disorder.
Therapeutic Strategies: Hydratases are potential therapeutic targets for various diseases. Inhibitors of enoyl-CoA hydratase are being explored as treatments for obesity and metabolic syndrome.
Development: Hydratases are essential for embryonic development and cellular differentiation. For instance, aconitase activity is crucial for the proper development of the nervous system.
Aging: The activity of hydratases declines with age, contributing to metabolic dysregulation and age-related diseases. Enhancing hydratase activity is being explored as a strategy to promote healthy aging.
Disease: Dysregulation of hydratase activity is implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Understanding the role of hydratases in disease pathogenesis can inform the development of novel therapeutic approaches.
