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Maltase is one type of alpha-glucosidase enzymes located in the brush border of the small intestine. This enzyme catalyzes the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltase is found in plants, bacteria, yeast, humans, and other vertebrates. It is thought to be synthesized by cells of the mucous membrane lining the intestinal wall.
Raffinose is a trisaccharide composed of galactose, glucose, and fructose. It can be found in beans, cabbage, brussels sprouts, broccoli, asparagus, other vegetables, and whole grains. Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme which in the lumen of the human digestive tract is only produced by bacteria in the large intestine. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. The enzyme does not cleave β-linked galactose, as in lactose.
α-Galactosidase is a glycoside hydrolase enzyme that catalyses the following reaction:
Sialyltransferases are enzymes that transfer sialic acid to nascent oligosaccharide. Each sialyltransferase is specific for a particular sugar substrate. Sialyltransferases add sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.
The term glycosynthase refers to a class of proteins that have been engineered to catalyze the formation of a glycosidic bond. Glycosynthase are derived from glycosidase enzymes, which catalyze the hydrolysis of glycosidic bonds. They were traditionally formed from retaining glycosidase by mutating the active site nucleophilic amino acid to a small non-nucleophilic amino acid. More modern approaches use directed evolution to screen for amino acid substitutions that enhance glycosynthase activity.
In enzymology, a galactose-6-sulfurylase is an enzyme that catalyzes the chemical reaction
Agarase is an enzyme with systematic name agarose 4-glycanohydrolase. It is found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of carbon and enables their ability to thrive in the ocean.
Porphyran is a sulfated carbohydrate derived from red algae of the genus Porphyra.
In molecular biology, glycoside hydrolase family 92 is a family of glycoside hydrolases.
In molecular biology, glycoside hydrolase family 47 is a family of glycoside hydrolases.
In molecular biology, glycoside hydrolase family 36 is a family of glycoside hydrolases.
DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase is an enzyme with systematic name acetyl-CoA:dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase. This enzyme catalyses the following chemical reaction
DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase is an enzyme with systematic name dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
κ-Carrageenase is an enzyme with systematic name κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining). It catalyses the endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans
Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase. This enzyme catalyses the following chemical reaction
Iota-carrageenase is an enzyme with systematic name iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting). This enzyme catalyses the following chemical reaction
Rhamnogalacturonan hydrolase is an enzyme with systematic name rhamnogalacturonan alpha-D-GalA-(1->2)-alpha-L-Rha hydrolase. This enzyme catalyses the following chemical reaction
Rhamnogalacturonan rhamnohydrolase is an enzyme with systematic name rhamnogalacturonan oligosaccharide alpha-L-Rha-(1->4)-alpha-D-GalA rhamnohydrolase. This enzyme catalyses the following chemical reaction
Gellan tetrasaccharide unsaturated glucuronyl hydrolase (EC 3.2.1.179, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp beta-D-4-deoxy-Delta4-GlcAp hydrolase. This enzyme catalyses the following chemical reaction
Phocaeicola plebeius, formerly Bacteroides plebeius, is a microbe found in the human gut, most often found in Japan natives. It is able to digest porphyran, a polysacchide from Porphyra seaweed (nori) that humans cannot digest on their own. The porphyranase-encoding gene Bp1689 is believed to have been derived from the microbe Zobellia galactanivorans via horizontal gene transfer, as part of a gene cluster containing other carbohydrate-active enzymes.
References
- ↑ Sugano Y, Kodama H, Terada I, Yamazaki Y, Noma M (November 1994). "Purification and characterization of a novel enzyme, alpha-neoagarooligosaccharide hydrolase (alpha-NAOS hydrolase), from a marine bacterium, Vibrio sp. strain JT0107". Journal of Bacteriology. 176 (22): 6812–8. PMC 197048 . PMID 7961439.
