chemical-categories

Arabinoxylanase 5A from Clostridium thermocellum, Recombinant LAB GRADE >90%

A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages.

UDP-acetylglucosamine deacetylase from Escherichia coli, Recombinant LAB GRADE 1

UDP-acetylglucosamine deacetylase is a metal-dependent deacetylase from Escherichia coli that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3.

UDP-acetylglucosamine deacetylase is a metal-dependent deacetylase from Escherichia coli that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3.

Exo-pectate lyase from Dickeya dadantii, Recombinant LAB GRADE >90% as judged by SDS-PAGE

In enzymology, a pectate disaccharide-lyase (EC 4.2.2.9) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

In enzymology, a pectate disaccharide-lyase (EC 4.2.2.9) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

Peptidoglycan N-acetylglucosamine deacetylase from Streptococcus pneumoniae, Recombinant LAB GRADE 1

Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N-acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O → peptidoglycan-D-glucosamine + acetate. This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.

Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N-deacetylase) is an enzyme with systematic name peptidoglycan-N-acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction: peptidoglycan-N-acetyl-D-glucosamine + H2O → peptidoglycan-D-glucosamine + acetate. This enzyme contributes to virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis.

Lytic cellulose monooxygenase from Thermobifida fusca, Recombinant LAB GRADE >90% as judged by SDS-PAGE

Lytic chitin monooxygenase is a copper-dependent lytic polysaccharide monooxygenase (LPMO). Copper-dependent lytic polysaccharide monooxygenases (LPMOs) are key players in the enzymatic conversion of biomass. LPMOs catalyze oxidative cleavage of glycosidic bonds in a process involving molecular oxygen and an electron donor, such as cellobiose dehydrogenase (CDH).

Lytic chitin monooxygenase is a copper-dependent lytic polysaccharide monooxygenase (LPMO). Copper-dependent lytic polysaccharide monooxygenases (LPMOs) are key players in the enzymatic conversion of biomass. LPMOs catalyze oxidative cleavage of glycosidic bonds in a process involving molecular oxygen and an electron donor, such as cellobiose dehydrogenase (CDH).

Poly ?-guluronate lyase from Zobellia galactanivorans, Recombinant LAB GRADE >90% as judged by SDS-PAGE

In enzymology, a poly(alpha-L-guluronate) lyase (EC 4.2.2.11) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing a terminal alpha-L-guluronate group, to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

In enzymology, a poly(alpha-L-guluronate) lyase (EC 4.2.2.11) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing a terminal alpha-L-guluronate group, to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

OligogalacOligogalacturonate lyase from Dickeya dadantii, Recombinantturonate lyase LAB GRADE >90% as judged by SDS-PAGE

In enzymology, an oligogalacturonide lyase (EC 4.2.2.6) is an enzyme that catalyzes the chemical reaction: 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate → 2 5-dehydro-4-deoxy-D-glucuronate. Hence, this enzyme has one substrate, 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate, and one product, 5-dehydro-4-deoxy-D-glucuronate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

In enzymology, an oligogalacturonide lyase (EC 4.2.2.6) is an enzyme that catalyzes the chemical reaction: 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate → 2 5-dehydro-4-deoxy-D-glucuronate. Hence, this enzyme has one substrate, 4-(4-deoxy-beta-D-gluc-4-enuronosyl)-D-galacturonate, and one product, 5-dehydro-4-deoxy-D-glucuronate. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.