| Galactose-6-sulfurylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.5 | ||||||||
| CAS no. | 9030-36-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a galactose-6-sulfurylase (EC 2.5.1.5) is an enzyme that catalyzes the chemical reaction
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is D-galactose-6-sulfate:alkyltransferase (cyclizing). Other names in common use include porphyran sulfatase, galactose-6-sulfatase, and galactose 6-sulfatase.
In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
Galactokinase is an enzyme (phosphotransferase) that facilitates the phosphorylation of α-D-galactose to galactose 1-phosphate at the expense of one molecule of ATP. Galactokinase catalyzes the second step of the Leloir pathway, a metabolic pathway found in most organisms for the catabolism of α-D-galactose to glucose 1-phosphate. First isolated from mammalian liver, galactokinase has been studied extensively in yeast, archaea, plants, and humans.
Glycosaminoglycans (GAGs) or mucopolysaccharides are long, linear polysaccharides consisting of repeating disaccharide units. The repeating two-sugar unit consists of a uronic sugar and an amino sugar, except in the case of the sulfated glycosaminoglycan keratan, where, in place of the uronic sugar there is a galactose unit. GAGs are found in vertebrates, invertebrates and bacteria. Because GAGs are highly polar molecules and attract water; the body uses them as lubricants or shock absorbers.
Galactose-1-phosphate uridyltransferase is an enzyme responsible for converting ingested galactose to glucose.
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins. In this form, HS binds to a variety of protein ligands, including Wnt, and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB, and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus. One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.
Cerebroside-sulfatase (EC 3.1.6.8, arylsulfatase A, cerebroside sulfate sulfatase) is an enzyme with systematic name cerebroside-3-sulfate 3-sulfohydrolase. This enzyme catalyses the following chemical reaction
Steroid sulfatase (STS), or steryl-sulfatase, formerly known as arylsulfatase C, is a sulfatase enzyme involved in the metabolism of steroids. It is encoded by the STS gene.
In biochemistry, sulfatases EC 3.1.6.- are a class of enzymes of the esterase class that catalyze the hydrolysis of sulfate esters into an alcohol and a bisulfate:
Arylsulfatase B is an enzyme associated with mucopolysaccharidosis VI.
Arylsulfatase (EC 3.1.6.1, sulfatase, nitrocatechol sulfatase, phenolsulfatase, phenylsulfatase, p-nitrophenyl sulfatase, arylsulfohydrolase, 4-methylumbelliferyl sulfatase, estrogen sulfatase) is a type of sulfatase enzyme with systematic name aryl-sulfate sulfohydrolase. This enzyme catalyses the following chemical reaction
Iduronate 2-sulfatase is a sulfatase enzyme associated with Hunter syndrome. It catalyses hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.
UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase is an enzyme involved in carbohydrate metabolism. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e.,
In enzymology, a N-sulfoglucosamine sulfohydrolase (EC 3.10.1.1), otherwise known as SGSH, is an enzyme that catalyzes the chemical reaction
The enzyme disulfoglucosamine-6-sulfatase (EC 3.1.6.1) catalyzes the reaction
The enzyme N-acetylgalactosamine-6-sulfatase catalyzes the chemical reaction of cleaving off the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of the macromolecule chondroitin sulfate and, similarly, of the D-galactose 6-sulfate units of the macromolecule keratan sulfate.
Galactose-3-O-sulfotransferase 4 is an enzyme that in humans is encoded by the GAL3ST4 gene.
Multiple sulfatase deficiency (MSD), also known as Austin disease, or mucosulfatidosis, is a very rare autosomal recessive lysosomal storage disease caused by a deficiency in multiple sulfatase enzymes, or in formylglycine-generating enzyme, which activates sulfatases. It is similar to mucopolysaccharidosis.
Porphyran is a sulfated carbohydrate derived from red algae of the genus Porphyra.
Formylglycine-generating enzyme (FGE), located at 3p26.1 in humans, is the name for an enzyme present in the endoplasmic reticulum that catalyzes the conversion of cysteine to formylglycine (fGly). There are two main classes of FGE, aerobic and anaerobic. FGE activates sulfatases, which are essential for the degradation of sulfate esters. The catalytic activity of sulfatases is dependent upon a formylglycine residue in the active site.
Beta porphyranase is an enzyme responsible for the degradation of porphyran, which composes the cell wall of red algae. So far only five β-porphyranases have been identified: PorA and PorB are found in the marine bacteria Zobellia galactinovirans. A wild-type porphyranase activity has been found in Pseudoalteromonas atlantica. BpGH16B and BpGH86A have been found in the human gut bacterium, Bacteroides plebeius, of Japanese individuals.
