Enzymes
Product List
HIBCH Human
3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant
HIBCH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
LTA4H Human
Leukotriene A4 Hydrolase Human Recombinant
LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PAFAH1B3 Human
Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant
PAFAH1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PAFAH2 Human
Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant
PAFAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
PTRH2 Human
Peptidyl-tRNA Hydrolase 2 Human Recombinant
PTRHD1 Human
Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant
PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ABHD10 Human
Abhydrolase Domain Containing 10 Human Recombinant
ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ABHD14B Human
Abhydrolase Domain Containing 14B Human Recombinant
ABHD14B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ACY1 Human
Aminoacylase-1 Human Recombinant
ACY1 Mouse
AminoAcylase-1 Mouse Recombinant
ACY1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Hydrolases are a class of enzymes that catalyze the hydrolysis of chemical bonds. These enzymes are essential for various biological processes, as they facilitate the breakdown of complex molecules into simpler ones by adding water. Hydrolases are classified based on the type of bond they act upon:
- Esterases: Hydrolyze ester bonds.
- Glycosidases: Hydrolyze glycosidic bonds in carbohydrates.
- Peptidases: Hydrolyze peptide bonds in proteins.
- Lipases: Hydrolyze lipid molecules.
- Phosphatases: Hydrolyze phosphate esters.
Key Biological Properties: Hydrolases exhibit high specificity for their substrates and operate under mild physiological conditions. They are often regulated by factors such as pH, temperature, and the presence of cofactors or inhibitors.
Expression Patterns: The expression of hydrolases varies widely among different organisms and tissues. Some hydrolases are constitutively expressed, while others are inducible in response to specific stimuli.
Tissue Distribution: Hydrolases are distributed throughout various tissues in the body. For example, digestive hydrolases like amylase and lipase are predominantly found in the pancreas and salivary glands, while lysosomal hydrolases are present in almost all cell types.
Primary Biological Functions: Hydrolases play crucial roles in metabolism, digestion, and cellular maintenance. They are involved in the degradation of macromolecules, recycling of cellular components, and energy production.
Role in Immune Responses: Certain hydrolases, such as lysozyme, are involved in the immune response by breaking down the cell walls of pathogens, thereby aiding in pathogen recognition and destruction.
Pathogen Recognition: Hydrolases can recognize and degrade pathogen-associated molecular patterns (PAMPs), which are essential for the innate immune response.
Mechanisms with Other Molecules and Cells: Hydrolases interact with various molecules and cells to exert their effects. For instance, digestive hydrolases break down dietary macromolecules into absorbable units.
Binding Partners: Hydrolases often require specific binding partners or cofactors to function effectively. For example, many hydrolases require metal ions like zinc or magnesium for catalytic activity.
Downstream Signaling Cascades: The activity of hydrolases can trigger downstream signaling cascades that regulate various cellular processes. For example, the hydrolysis of phosphoinositides by phospholipase C generates second messengers that modulate cellular signaling pathways.
Regulatory Mechanisms: The expression and activity of hydrolases are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.
Transcriptional Regulation: The transcription of hydrolase genes can be regulated by various transcription factors in response to environmental cues or cellular signals.
Post-Translational Modifications: Hydrolases can undergo post-translational modifications such as phosphorylation, glycosylation, and ubiquitination, which can alter their activity, stability, and localization.
Biomedical Research: Hydrolases are widely used in biomedical research to study metabolic pathways, disease mechanisms, and cellular processes.
Diagnostic Tools: Hydrolases serve as biomarkers for various diseases. For example, elevated levels of certain hydrolases in the blood can indicate liver or pancreatic disorders.
Therapeutic Strategies: Hydrolases are employed in therapeutic strategies, such as enzyme replacement therapy for lysosomal storage diseases and the use of proteases in wound debridement.
Role Throughout the Life Cycle: Hydrolases play vital roles throughout the life cycle, from development to aging and disease. During development, hydrolases are involved in tissue remodeling and differentiation. In adulthood, they maintain cellular homeostasis and metabolic balance. In aging and disease, dysregulation of hydrolase activity can contribute to pathological conditions such as neurodegeneration and cancer.
