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.
X-linked ichthyosis is a skin condition caused by the hereditary deficiency of the steroid sulfatase (STS) enzyme that affects 1 in 2000 to 1 in 6000 males. XLI manifests with dry, scaly skin and is due to deletions or mutations in the STS gene. XLI can also occur in the context of larger deletions causing contiguous gene syndromes. Treatment is largely aimed at alleviating the skin symptoms. The term is from the Ancient Greek 'ichthys' meaning 'fish'.
Arylsulfatase A is an enzyme that breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. In humans, arylsulfatase A is encoded by the ARSA gene.
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.
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.
N-acetylgalactosamine-4-sulfatase is an enzyme with systematic name N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase. It catalyses the following reaction:
N-acetylgalactosamine-6-sulfatase is an enzyme that, in humans, is encoded by the GALNS gene.
N-acetylglucosamine-6-sulfatase (EC 3.1.6.14, glucosamine (N-acetyl)-6-sulfatase, systematic name N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase) is an enzyme that in humans is encoded by the GNS gene. It is deficient in Sanfilippo Syndrome type IIId. It catalyses the hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate
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 chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
The enzyme cellulose-polysulfatase catalyzes hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin.
In enzymology, a galactose-6-sulfurylase is an enzyme that catalyzes the chemical reaction
Sulfatase 1, also known as SULF1, is an enzyme which in humans is encoded by the SULF1 gene.
Arylsulfatase L is an enzyme that, in humans, is encoded by the ARSL gene.
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.
Irosustat is an orally active, irreversible, nonsteroidal inhibitor of steroid sulfatase (STS) and member of the aryl sulfamate ester class of drugs that was under development by Sterix Ltd and Ipsen for the treatment of hormone-sensitive cancers such as breast cancer, prostate cancer, and endometrial cancer but has not yet been marketed. The drug was first designed and synthesized in the group of Professor Barry V L Potter at the Department of Pharmacy & Pharmacology, University of Bath, working together with Professor Michael J. Reed at Imperial College, London and its initial development was undertaken through the university spin-out company Sterix Ltd and overseen by Cancer Research UK (CRUK). Results of the "first-in-class" clinical trial in breast cancer of an STS inhibitor in humans were published in 2006 and dose optimisation studies and further clinical data have been reported.
Estradiol sulfamate, or estradiol-3-O-sulfamate, is a steroid sulfatase (STS) inhibitor which is under development for the treatment of endometriosis. It is the C3 sulfamate ester of estradiol, and was originally thought to be a prodrug of estradiol. The drug was first synthesized as an STS inhibitor along with its oxidized version estrone 3-O-sulfamate (EMATE) in the group of Professor Barry V L Potter at the University of Bath, UK, working together with Professor Michael J Reed at Imperial College, London and was found to be highly estrogenic in rodents. Such aryl sulfamate esters were shown to be "first-in-class" highly potent active site-directed irreversible STS inhibitors. Compounds of this class are thought to irreversibly modify the active site formylglycine residue of STS. The drug shows profoundly reduced susceptibility to first-pass metabolism relative to estradiol, and was believed to be the first "potent" estradiol prodrug to be discovered. It was clinically investigated for possible use as an estrogen for indications like hormonal contraception and menopausal hormone therapy. However, it showed no estrogenic effects in women. The potent non-estrogenic clinical STS inhibitor Irosustat (STX64/667-Coumate) was used to explore the possibility that STS might be responsible for the hydrolysis of estrogen sulphamates. Results demonstrated convincingly that STS is the enzyme responsible for the removal of the sulfamoyl group from estrogen sulfamates and has a crucial role in regulating the estrogenicity associated with this class of drug. Thus, STS inhibition blocks the conversion of E2MATE into estradiol and thereby abolishes its estrogenicity in humans. Irosustat has completed a number of clinical trials in oncology as an STS inhibitor currently up to Phase II.
