lyase

(-)-Hydroxycitric acid (Garcinia acid) is the principal acid found in the fruit rinds of Garcinia cambogia. It acts as a potent and competitive inhibitor of ATP citrate lyase, suppressing fatty acid synthesis, food intake, lipogenesis, and inducing weight loss.

OGG1-IN-08 (OGG1-IN-O8) is an inhibitor of 8-oxoguanine DNA glycosylase 1 (OGG1;IC50 : 0.35 μM)

Cystathionine-γ-lyase-IN-1 (SHIP-2a) is a selective inhibitor of cystathionine γ-lyase (CSE) enzyme (IC50= 6.3 μM).

N-Acetylneuraminate lyase (CgNal) (Sialic acid aldolase (CgNal)), a class I aldolase frequently utilized in biochemical research, catalyzes the reversible condensation of pyruvate and N-acetyl-d-mannosamine (ManNAc), producing N-acetylneuraminic acid (Neu5Ac) [1].

Pectate Lyase, an enzyme secreted by plant pathogens, is essential for pectin degradation and plays a vital role in fungal virulence. Additionally, it triggers plant immune responses, further contributing to its virulence [1].

Pectate Lyase, Clostridium acetobutylicum (EC 4.2.2.2), is an enzyme involved in the soft rot of plant tissues. It facilitates the eliminative cleavage of polygalacturonic acid, resulting in oligosaccharides that possess non-reducing ends with 4-deoxy-α-D-mann-4-enuronosyl groups.

Phenylalanine Ammonia-Lyase from Rhodotorula glutinis (EC 4.3.1.24) can be inactivated by proteolytic cleavage with enzymes such as trypsin-chymotrypsin, Bacillus subtilis proteinase, and trypsin.

Pectate Lyase, from Cellvibrio japonicus (EC 4.2.2.2), is an enzyme that contributes to the soft rot of plant tissues. It catalyzes the eliminative cleavage of polygalacturonic acid, resulting in the formation of oligogalacturonides with a non-reducing end containing the 4-deoxy-α-D-mann-4-enuronosyl group.

Pectate Lyase, Aspergillus sp. (EC 4.2.2.2), is an enzyme involved in the breakdown of plant tissues, leading to soft rot. It catalyzes the lyase reaction of pectic acid, resulting in the formation of oligosaccharides with a non-reducing end containing the 4-deoxy-α-D-mann-4-enuronic acid group.

Xanthan lyase, Bacillus sp. (EC 4.2.2.12), is an enzyme that catalyzes the cleavage of β-D-mannosyl-β-D-1,4-glucuronic acid bonds in the polysaccharide xanthan. This enzyme is part of the family of lyases, specifically carbon-oxygen lyases that target polysaccharides.

Pectate Lyase, Caulobacter crescentus (EC 4.2.2.2), is an enzyme involved in the soft rot of plant tissues. It catalyzes the eliminative cleavage of polygalacturonic acid, producing oligomers that have non-reducing ends with 4-deoxy-α-D-mann-4-enuronosyl groups.

Citrate Lyase, Klebsiella pneumoniae (EC 4.1.3.6), catalyzes the initial step of citrate degradation, forming acetate and oxaloacetate. It comprises three polypeptide subunits: the α subunit, which functions as a transferase; the β subunit, acting as an acyl-lyase; and the γ subunit, serving as an acyl-carrier protein.

(2R)-Sulfolactate sulfo-lyase (EC 4.4.1.24) is an inducible enzyme involved in the degradation of cysteine by Paracoccus NKNCYSA and the breakdown of 3-sulfolactate by Halomonas. It exhibits specificity for the (R) isomer of its substrate.

β-Alanyl-CoA ammonia-lyase (EC 4.3.1.6) is an enzyme that belongs to the lyase family, specifically the ammonia-lyases, which are responsible for breaking carbon-nitrogen bonds.

(S)-Hydroxynitrile lyase [EC 4.1.2.47] catalyzes the cleavage of hydroxynitriles into cyanide and their corresponding aldehyde or ketone.

α-D-Ribose 1-methylphosphonate 5-phosphate C-P-lyase (EC 4.7.1.1), isolatable from Escherichia coli, involves a [4Fe-4S] cluster and a S-adenosyl-L-methionine (SAM) radical.

(R)-Citramalyl-CoA lyase (EC 4.1.3.46) requires Mn2+ ions for its activity and does not exhibit activity towards (3S)-citramalyl-CoA.

Alginate lyase, Sphingomonas sp. (EC 4.2.2.3), is an enzyme that catalyzes the elimination reaction of polysaccharides containing β-D-mannuronic acid residues, resulting in oligosaccharides with terminal 4-deoxy-α-L-erythro-hex-4-enopyranosyluronic acid groups. This enzyme is part of the lyase family and plays a role in the metabolism of fructose and mannose.

(S)-cheilanthifoline synthase (EC 1.14.21.2) catalyzes an oxidation reaction in which oxygen is not incorporated into the product.

Cystathionine β-lyase is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that cleaves the Cβ-Sγ bond of cystathionine to convert L-cysteine into L-homocysteine. Cystathionine β-lyase is involved in the de novo synthesis of methionine in microorganisms and plants and plays an important role in bacterial virulence.

L-Methionine γ-lyase (Methionine lyase), a multifaceted enzyme in the γ-family of pyridoxal-5'-phosphate (PLP)-dependent enzymes, catalyzes the α, γ-elimination of L-methionine and homocysteine. This enzyme exhibits anticancer and anti-infectious properties and is utilized in homocysteinemia research [1][2][3].

Alginate lyase is a biochemical reagent utilized in life sciences research and can function as either a biomaterial or an organic compound.

Citrate lyase is an enzyme that converts citric acid into oxaloacetate.

L-Methionine γ-lyase, pseudomonas putida, is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on improving enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions (such as low or high pH). Introducing stimuli-responsive modifications to these enzymes allows for the dynamic control of their activity.