Enzymes
Product List
ADSL Human
Adenylosuccinate Lyase Human Recombinant
ADSL is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ASL Human
Argininosuccinate Lyase Human Recombinant
ASL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CCBL1 Human
Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant
CTH Human
Cystathionase Human Recombinant
CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HMGCL Human
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant
HMGCL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HMGCL Human, Sf9
3-Hydroxymethyl-3-Methylglutaryl-CoA Lyase Human Recombinant, Sf9
HMGCL Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 305 amino acids (28-325 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HMGCL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
NANA E.Coli
N-Acetylneuraminate Lyase E.Coli Recombinant
NANA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
NPL Human
N-acetylneuraminate Pyruvate Lyase Human Recombinant
NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SRR Human
Serine Racemase Human Recombinant
SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Lyases are a class of enzymes that catalyze the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure . They are classified under the EC number classification as EC 4 and can be further divided into several subclasses based on the type of bond they cleave:
Lyases exhibit diverse biological properties, including specific expression patterns and tissue distribution. For instance, alginate lyases are found in various organisms such as algae, marine mollusks, and bacteria . These enzymes play crucial roles in the degradation of alginate, a polysaccharide found in the cell walls of brown algae . The expression of lyases can be tissue-specific, and their activity can be influenced by environmental factors and developmental stages .
The primary biological functions of lyases include the catalysis of bond cleavage in various biochemical pathways. For example, phenylalanine ammonia lyase (PAL) is involved in the phenylpropanoid pathway, which is essential for the production of secondary metabolites like flavonoids and lignin . Lyases also play roles in immune responses and pathogen recognition. For instance, alginate lyases can degrade the alginate produced by pathogenic bacteria, aiding in the host’s defense mechanisms .
Lyases operate through mechanisms that involve the breaking of chemical bonds without the addition of water or transfer of electrons. For example, pectate lyases cleave the α-1,4-glycosidic bond of pectin molecules through a β-elimination reaction, producing pectin oligosaccharides . These enzymes often have specific binding partners and can initiate downstream signaling cascades that regulate various cellular processes .
The expression and activity of lyases are tightly regulated through various mechanisms. Transcriptional regulation involves the binding of transcription factors to promoter regions of lyase genes, as seen with phenylalanine ammonia lyase (PAL) in plants . Post-translational modifications, such as phosphorylation, can also modulate the activity of lyases, ensuring their proper function in response to cellular signals .
Lyases have significant applications in biomedical research, diagnostics, and therapeutic strategies. Alginate lyases, for instance, are used in the production of biofuels and biochemicals from alginate . They also have potential applications in tissue engineering and wound healing due to their ability to degrade alginate-based biofilms . In diagnostics, lyases can be used as biomarkers for certain diseases, and their inhibitors can serve as therapeutic agents .
Throughout the life cycle, lyases play essential roles in development, aging, and disease. For example, isocitrate lyase (ICL) is crucial for plant salt tolerance and is highly expressed during stress conditions . In humans, lyases are involved in metabolic pathways that are critical for growth and development. Dysregulation of lyase activity can lead to various diseases, highlighting their importance in maintaining cellular homeostasis .
