An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.
Fucose is a deoxyhexose sugar, specifically a L-configuration 6-deoxygalactose, often found as a component of complex carbohydrates called glycans in various glycoproteins and glycolipids within the human body.
An autosomal recessive lysosomal storage disease caused by a deficiency of ALPHA-L-FUCOSIDASE activity resulting in an accumulation of fucose containing SPHINGOLIPIDS; GLYCOPROTEINS, and mucopolysaccharides (GLYCOSAMINOGLYCANS) in lysosomes. The infantile form (type I) features psychomotor deterioration, MUSCLE SPASTICITY, coarse facial features, growth retardation, skeletal abnormalities, visceromegaly, SEIZURES, recurrent infections, and MACROGLOSSIA, with death occurring in the first decade of life. Juvenile fucosidosis (type II) is the more common variant and features a slowly progressive decline in neurologic function and angiokeratoma corporis diffusum. Type II survival may be through the fourth decade of life. (From Menkes, Textbook of Child Neurology, 5th ed, p87; Am J Med Genet 1991 Jan;38(1):111-31)
An integrin heterodimer widely expressed on cells of hematopoietic origin. CD11A ANTIGEN comprises the alpha chain and the CD18 antigen (ANTIGENS, CD18) the beta chain. Lymphocyte function-associated antigen-1 is a major receptor of T-CELLS; B-CELLS; and GRANULOCYTES. It mediates the leukocyte adhesion reactions underlying cytolytic conjugate formation, helper T-cell interactions, and antibody-dependent killing by NATURAL KILLER CELLS and granulocytes. Intracellular adhesion molecule-1 has been defined as a ligand for lymphocyte function-associated antigen-1.
Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
Cell-surface glycoprotein beta-chains that are non-covalently linked to specific alpha-chains of the CD11 family of leukocyte-adhesion molecules (RECEPTORS, LEUKOCYTE-ADHESION). A defect in the gene encoding CD18 causes LEUKOCYTE-ADHESION DEFICIENCY SYNDROME.
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Adherence of cells to surfaces or to other cells.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

Endometrial lysosomal enzyme activity in normal cycling endometrium. (1/168)

The objective of this study was to evaluate the possible role of four lysosomal enzymes in endometrial function and remodelling during the normal menstrual cycle by fluorimetric measurement (acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and alpha-D-mannosidase). A prospective study was conducted of 45 endometrial biopsies obtained from women with normal menstrual cycles. Activity of all four enzymes was identified in human endometrium. Activity of acid phosphatase and N-acetyl-beta-D-glucosaminidase was relatively high, whilst that of alpha-L-fucosidase and alpha-D-mannosidase was low. There was no significant change in the activity of any of the four enzymes from the proliferative to the secretory phase of the cycle. This study suggests that the activity of these enzymes remains constant throughout a major portion of the normal cycle.  (+info)

Characterization of human semen alpha-L-fucosidases. (2/168)

Human semen contains a large amount of alpha-L-fucosidase activity, the great majority of which is found in the seminal fluid. Immunocytochemical studies indicate that a small amount of semen fucosidase activity is present on the sperm plasma membrane, primarily in the posterior head region. Subcellular fractionation studies also indicate that sperm alpha-L-fucosidase is present in the plasma membrane-enriched fraction. Comparative characterization of human seminal fluid and sperm alpha-L-fucosidases indicates that seminal fluid alpha-L-fucosidase has a broad pH optimum curve with a number of near-equal maxima between pH 4.8 and 7.0 while sperm fucosidase has a major optimum between pH 3.4 and 4.0. Isoelectric focusing indicates that seminal fluid alpha-L-fucosidase contains three to six isoforms with isoelectric points (pI) of 5-7 while sperm fucosidase contains two distinct isoforms with pI values of 5. 2 +/- 0.2 and 7.0 +/- 0.2. Western blotting indicates that seminal fluid fucosidase contains a major protein band with a molecular mass ratio (M(r)) of approximately 56 kDa while sperm fucosidase contains a major protein band of approximately 51 kDa. The overall results indicate the presence of a low-abundance, plasma membrane-associated human sperm alpha-L-fucosidase, which is different in its properties from human seminal fluid alpha-L-fucosidase(s), and whose function is not yet known.  (+info)

Fucose in alpha(1-6)-linkage regulates proliferation and histogenesis in reaggregated retinal spheroids of the chick embryo. (3/168)

We have used the lectin from Aleuria aurantia (AAL) which is highly specific for alpha(1-6)-linked fucose, to examine its effect on chicken retinogenesis in a reaggregation culture system. When dispersed cells of the embryonic chick retina are reaggregated to form histotypic retinospheroids, AAL elicits strong inhibition of spheroid growth. The action of AAL is specific, since its effect is dose-dependent, saturable, and inhibited by an excess of fucose. Fucosidase treatment entirely abolishes reaggregation. In contrast, Anguilla anguilla agglutinin (AAA) binding to fucose in alpha(1-2)-linkage does not show any effects. Incubation with CAB4-a specific monoclonal antibody for fucose in alpha(1-6)-linkage-reduces spheroid size and shape. AAL does not much affect primary aggregation, but rather subsequent processes of cell proliferation and histogenesis. In particular, AAL inhibits uptake of bromo-desoxyuridine (BrdU), most efficiently so during days in vitro 2 (div2) and div3. As a consequence, the histological differentiation is entirely disturbed, as evidenced by vimentin immunostaining; particularly, rosettes are not forming and the radial glia scaffold is disorganized. We conclude that glycoproteins exhibiting fucose in alpha(1-6)-linkage may play major roles in early processes of retinal tissue formation.  (+info)

Glycosylation alterations of cells in late phase apoptosis from colon carcinomas. (4/168)

Comparisons of carbohydrate profiles between control and apoptotic colon carcinoma cells were performed by flow cytometry using a set of lectins and anti-carbohydrate antibodies. The six cell lines analyzed presented distinct carbohydrate profiles before induction of apoptosis. PHA-L and MAA binding decreased after induction of apoptosis by UV-treatment. In contrast an increase of PNA binding was observed after induction of apoptosis, except on SW-48 cells for which a decrease occurred. A decrease of SNA binding was observed after induction of apoptosis from strongly positive control cell lines, whereas it increased on weakly positive ones. All the blood group related antigens A, H, Lewis a, Lewis x, Lewis b, and Lewis y, had their expression strongly diminished on apoptotic cells. These changes occurred irrespective of the mode of apoptosis induction since similar results were obtained after UV, TNFalpha, or anti-Fas treatment. Fucosyltransferases activities were also decreased after apoptosis induction, except for alpha1,3fucosyltransferase in anti-Fas treated HT-29 cells, where it was strongly augmented. This could be attributed to the IFNgamma preteatment required to induce Fas expression on these cells. Fucosidase activity decreased after induction of apoptosis suggesting that it was not responsible for the loss of fucosylated structures. In the rat PRO cell line, H blood group antigens are mainly carried by a high molecular weight variant of CD44. It could be shown that the loss of H antigen after induction of apoptosis correlated with a loss of the carrier glycoprotein.  (+info)

Terminal glycosylation in cystic fibrosis. (5/168)

Cystic fibrosis (CF) is a common genetic disease for which the gene was identified within the last decade. Pulmonary disease predominates in this ultimately fatal disease and current therapy only slows the progression. CF transmembrane regulator (CFTR), the gene product, is an integral membrane glycoprotein that normally functions as a chloride channel in epithelial cells. The most common mutation, deltaF508, results in mislocalization and altered glycosylation of CFTR. Altered fucosylation and sialylation are hallmarks of both membrane and secreted glycoproteins in CF and the focus here is on these investigations. Oligosaccharides from CF membrane glycoproteins have the Lewis x, selectin ligand in terminal positions. In addition, two major bacterial pathogens in CF, Pseudomonas aeruginosa and Haemophilus influenzae, have binding proteins, which recognize fucose in alpha1,3 linkage and asialoglycoconjugates. We speculate that the altered terminal glycosylation of airway epithelial glycoproteins in CF contributes to the chronic infection and robust inflammatory response in the CF lung. Understanding the effects of mutant CFTR on glycosylation may provide further insight into the regulation of glycoconjugate processing as well as therapy for CF.  (+info)

Prediction of the development of hepato-cellular-carcinoma in patients with liver cirrhosis by the serial determinations of serum alpha-L-fucosidase activity. (6/168)

OBJECTIVE: Evaluation of the usefulness of the serial determinations of serum alpha-L-fucosidase (AFU) activity for prediction of the development of hepatocellular carcinoma (HCC) was performed. METHODS AND PATIENTS: Serum AFU activity was determined monthly for 42 months in 73 patients with liver cirrhosis (LC). RESULTS: HCC was diagnosed in 27 patients by means of ultrasonography during this observation period. In 23 (85%) of the 27 patients, serum AFU activity was found to exceed 700 nmole/ml/h during the LC stage. HCC developed within a few years in 23 (82%) of 28 LC patients with AFU activity exceeding 700 nmole/ml/h, in contrast, it developed in only 4 (9%) of 45 LC patients with AFU activity below 700 nmole/ml/h. AFU activity was already elevated in 23 (85%) of 27 patients at least 6 months before the detection of HCC by ultrasonography. CONCLUSION: It is conceivable that the development of HCC can be predicted by means of serial determinations of serum AFU activity in patients with LC.  (+info)

Endometrial lysosomal enzyme activity in ovulatory dysfunctional uterine bleeding, IUCD users and post-partum women. (7/168)

The aim of this study was to evaluate the role of lysosomal enzymes in excessively heavy menstruation by comparing women with menorrhagia due to dysfunctional bleeding or intrauterine contraceptive device (IUCD) use with those with normal menstrual periods or with amenorrhoea associated with breastfeeding. This was a prospective cohort investigation of the activity of four endometrial lysosomal enzymes in three contrasting groups: (i) women with ovulatory dysfunctional uterine bleeding and users of intrauterine contraceptive devices; (ii) breastfeeding post-partum women in whom there are long periods of amenorrhoea, particularly in the early months post-partum; and (iii) normal cycling women. It was found that the total activity of lysosomal enzymes, particularly acid phosphatase and N-acetyl-beta-D-glucosaminidase, was markedly elevated (P < 0.001) in IUCD-exposed endometrium, and endometrium from women with dysfunctional uterine bleeding when compared with endometrium from women with a history of entirely normal menstrual periods or that in post-partum breastfeeding women. The activity of alpha-L-fucosidase was moderately elevated in IUCD users (P < 0.05) and ovulatory dysfunctional uterine bleeding (P < 0.05), whereas alphaD-mannosidase activity was elevated in ovulatory dysfunctional uterine bleeding (P < 0.05), but decreased in IUCD users (P < 0.01). No significant differences were observed in the lysosomal enzyme activities of breastfeeding post-partum women and normal cycling women. These results show that total endometrial tissue activity of four lysosomal enzymes was substantially increased throughout the cycle in most circumstances in women with two different causes for increased menstrual bleeding. This suggests a contributory role to the increased bleeding.  (+info)

Sequence and expression of Thai Rosewood beta-glucosidase/beta-fucosidase, a family 1 glycosyl hydrolase glycoprotein. (8/168)

Dalcochinin-8'-O-beta-glucoside beta-glucosidase (dalcochinase) from the Thai rosewood (Dalbergia cochinchinensis Pierre) has aglycone specificity for isoflavonoids and can hydrolyze both beta-glucosides and beta-fucosides. To determine its structure and evolutionary lineage, the sequence of the enzyme was determined by peptide sequencing followed by PCR cloning. The cDNA included a reading frame coding for 547 amino acids including a 23 amino acid propeptide and a 524 amino acid mature protein. The sequences determined at peptide level were found in the cDNA sequence, indicating the sequence obtained was indeed the dalcochinase enzyme. The mature enzyme is 60% identical to the cyanogenic beta-glucosidase from white clover glycosyl hydrolase family 1, for which an X-ray crystal structure has been solved. Based on this homology, residues which may contribute to the different substrate specificities of the two enzymes were identified. Eight putative glycosylation sites were identified, and one was confirmed to be glycosylated by Edman degradation and mass spectrometry. The protein was expressed as a prepro-alpha-mating factor fusion in Pichia pastoris, and the activity of the secreted enzyme was characterized. The recombinant enzyme and the enzyme purified from seeds showed the same K(m) for pNP-glucoside and pNP-fucoside, had the same ratio of V(max) for these substrates, and similarly hydrolyzed the natural substrate, dalcochinin-8'-beta-glucoside.  (+info)

Alpha-L-Fucosidase is an enzyme that catalyzes the hydrolysis of the terminal alpha-L-fucose residues from glycoproteins, glycolipids, and other substrates. This enzyme plays a crucial role in the degradation and recycling of complex carbohydrates found on the surface of cells and in various biological fluids. Deficiencies in alpha-L-fucosidase activity can lead to genetic disorders such as fucosidosis, which is characterized by the accumulation of fucose-containing glycoproteins and glycolipids in various tissues and organs, resulting in progressive neurological deterioration and other systemic manifestations.

Fucose is a type of sugar molecule that is often found in complex carbohydrates known as glycans, which are attached to many proteins and lipids in the body. It is a hexose sugar, meaning it contains six carbon atoms, and is a type of L-sugar, which means that it rotates plane-polarized light in a counterclockwise direction.

Fucose is often found at the ends of glycan chains and plays important roles in various biological processes, including cell recognition, signaling, and interaction. It is also a component of some blood group antigens and is involved in the development and function of the immune system. Abnormalities in fucosylation (the addition of fucose to glycans) have been implicated in various diseases, including cancer, inflammation, and neurological disorders.

Fucosidosis is a rare inherited metabolic disorder caused by the deficiency of the enzyme alpha-L-fucosidase. This enzyme is responsible for breaking down complex sugars called glycoproteins and glycolipids in the body. Without sufficient levels of this enzyme, these substances accumulate in various tissues and organs, leading to progressive cellular damage and impaired function.

The condition is characterized by a wide range of symptoms, including coarse facial features, developmental delays, intellectual disability, seizures, vision and hearing loss, cardiac problems, and skeletal abnormalities. There are two main types of fucosidosis, type 1 and type 2, which differ in the age of onset and severity of symptoms.

Fucosidosis is an autosomal recessive disorder, meaning that an individual must inherit two copies of the defective gene, one from each parent, to develop the condition. It is typically diagnosed through enzyme assays and genetic testing. Currently, there is no cure for fucosidosis, and treatment is focused on managing symptoms and improving quality of life.

Lymphocyte Function-Associated Antigen-1 (LFA-1) is a type of integrin, which is a family of cell surface proteins that are important for cell-cell adhesion and signal transduction. LFA-1 is composed of two subunits, called alpha-L (CD11a) and beta-2 (CD18), and it is widely expressed on various leukocytes, including T cells, B cells, and natural killer cells.

LFA-1 plays a crucial role in the immune system by mediating the adhesion of leukocytes to other cells, such as endothelial cells that line blood vessels, and extracellular matrix components. This adhesion is necessary for leukocyte migration from the bloodstream into tissues during inflammation or immune responses. LFA-1 also contributes to the activation of T cells and their interaction with antigen-presenting cells, such as dendritic cells and macrophages.

The binding of LFA-1 to its ligands, including intercellular adhesion molecule 1 (ICAM-1) and ICAM-2, triggers intracellular signaling pathways that regulate various cellular functions, such as cytoskeletal reorganization, gene expression, and cell survival. Dysregulation of LFA-1 function has been implicated in several immune-related diseases, including autoimmune disorders, inflammatory diseases, and cancer.

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

CD18 is a type of protein called an integrin that is found on the surface of many different types of cells in the human body, including white blood cells (leukocytes). It plays a crucial role in the immune system by helping these cells to migrate through blood vessel walls and into tissues where they can carry out their various functions, such as fighting infection and inflammation.

CD18 forms a complex with another protein called CD11b, and together they are known as Mac-1 or CR3 (complement receptor 3). This complex is involved in the recognition and binding of various molecules, including bacterial proteins and fragments of complement proteins, which help to trigger an immune response.

CD18 has been implicated in a number of diseases, including certain types of cancer, inflammatory bowel disease, and rheumatoid arthritis. Mutations in the gene that encodes CD18 can lead to a rare disorder called leukocyte adhesion deficiency (LAD) type 1, which is characterized by recurrent bacterial infections and impaired wound healing.

Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.

Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).

These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.

Integrin α4β1, also known as Very Late Antigen-4 (VLA-4), is a heterodimeric transmembrane receptor protein composed of two subunits, α4 and β1. It is involved in various cellular activities such as adhesion, migration, and signaling. This integrin plays a crucial role in the immune system by mediating the interaction between leukocytes (white blood cells) and the endothelial cells that line blood vessels. The activation of Integrin α4β1 allows leukocytes to roll along and then firmly adhere to the endothelium, followed by their migration into surrounding tissues, particularly during inflammation and immune responses. Additionally, Integrin α4β1 also interacts with extracellular matrix proteins such as fibronectin and helps regulate cell survival, proliferation, and differentiation in various cell types.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

... may refer to one of two enzymes: Fucosidase Alpha-L-fucosidase This set index page lists enzyme articles ...
The enzyme 1,3-α-L-fucosidase (EC 3.2.1.111) catalyzes the hydrolytic cleavage of the 1,3-linkages between α-L-fucose and N- ... Yoshima H, Takasaki S, Ito-Mega S, Kobata A (1979). "Purification of almond emulsin α-L-fucosidase I by affinity chromatography ... Ogata-Arakawa M, Muramatsu T, Kobata A (1977). "α-L-fucosidases from almond emulsin: characterization of the two enzymes with ... This enzyme is also called almond emulsin fucosidase I. It participates in the degradation of glycan structures. Imber MJ, ...
It is also called α-L-fucosidase. Yazawa S, Madiyalakan R, Chawda RP, Matta KL (1986). "α-L-fucosidase from Aspergillus niger: ... The enzyme 1,6-α-L-fucosidase (EC 3.2.1.127) catalyses the following chemical reaction Hydrolysis of 1,6-linkages between α-L- ... demonstration of a novel α-L-(1→6)-fucosidase acting on glycopeptides". Biochem. Biophys. Res. Commun. 136 (2): 563-9. doi: ...
Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks ... "Entrez Gene: FUCA1 fucosidase, alpha-L- 1, tissue". HPRD entry [1] Archived 2004-10-24 at the Wayback Machine Willems PJ, Gatti ... Fukushima H, de Wet JR, O'Brien JS (1985). "Molecular cloning of a cDNA for human alpha-L-fucosidase". Proc. Natl. Acad. Sci. U ... Yang M, Allen H, DiCioccio RA (1993). "A mutation generating a stop codon in the alpha-L-fucosidase gene of a fucosidosis ...
Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of ... Glycoside hydrolase family 29 includes alpha-L-fucosidases, They are lysosomal enzymes responsible for hydrolyzing the alpha-1, ... making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l- ... In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by ...
Plasma alpha-L-fucosidase (see alpha-L-fucosidase) is an enzyme that in humans is encoded by the FUCA2 gene. GRCh38: Ensembl ... "Entrez Gene: FUCA2 fucosidase, alpha-L- 2, plasma". Narahara K, Tsuji K, Yokoyama Y, et al. (1991). "Specification of small ... Eiberg H, Mohr J, Nielsen LS (Oct 1984). "Linkage of plasma alpha-L-fucosidase (FUCA2) and the plasminogen (PLG) system". Clin ... 2001). "Cell surface human alpha-L-fucosidase". Eur. J. Biochem. 268 (11): 3321-31. doi:10.1046/j.1432-1327.2001.02237.x. PMID ...
If they are present, a skin or blood sample will be taken to test for below-normal amounts of alpha-fucosidase. Fucosidosis is ... The gene encoding the alpha-fucosidase, FUCA 1, was found to be located to the short arm of chromosome 1p36 - p34, by Carrit ... The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. The enzyme plays a role in the breakdown ... The deficiency of the enzyme alpha-L-fucosidase, which is used to metabolize complex compounds in the body (fucose-containing ...
6-α-L-fucosidase FUCA2 Endreffy I, Bjørklund G, Szerafin L, Urbina MA, Chirumbolo S, Endreffy E. Plasma alpha-L-fucosidase ... doi: 10.1007/s12026-017-8943-x. Levvy GA, Mcallan A (August 1961). "Mammalian fucosidases. 2. α-L-Fucosidase". The Biochemical ... In CAZy, α-L-fucosidases are found in glycoside hydrolase family 29 and glycoside hydrolase family 95. As of late 2007, 3 ... Tanaka K, Nakano T, Noguchi S, Pigman W (August 1968). "Purification of α-L-fucosidase of abalone livers". Archives of ...
"Alpha fucosidase and beta galactosidase in serum of a Lyme disease patients as a possible marker of accelerated senescence - a ...
Zhang SY, Lin BD, Li BR (2015). "Evaluation of the diagnostic value of alpha-l-fucosidase, alpha-fetoprotein and thymidine ...
"An alpha-L-fucosidase from Penicillium multicolor as a candidate enzyme for the synthesis of alpha (1-->3)-linked fucosyl ... Penicillium multicolor is an anamorph species of the genus Penicillium which produces alpha-L-fucosidase, tilactase, ... Ajisaka, K.; Fujimoto, H.; Miyasato, M. (1998). "An α-l-fucosidase from Penicillium multicolor as a candidate enzyme for the ...
... alpha-L-fucosidase, poly(1,2-alpha-L-fucoside-4-sulfate) glycanohydrolase) is an enzyme with systematic name poly((1->2)-alpha- ... This enzyme catalyses the following chemical reaction Endohydrolysis of (1->2)-alpha-L-fucoside linkages in fucoidan without ...
... alpha-L-fucosidase MeSH D08.811.277.450.410 - galactosidases MeSH D08.811.277.450.410.050 - alpha-galactosidase MeSH D08.811. ... gtp-binding protein alpha subunits MeSH D08.811.277.040.330.300.200.100.100 - gtp-binding protein alpha subunits, g12-g13 MeSH ... gtp-binding protein alpha subunit, gi2 MeSH D08.811.277.040.330.300.200.100.300 - gtp-binding protein alpha subunits, gq-g11 ... steroid 12-alpha-hydroxylase MeSH D08.811.682.690.708.170.915.737 - steroid 16-alpha-hydroxylase MeSH D08.811.682.690.708.170. ...
... alpha/beta-galactosidase, β-glucuronidase, α-fucosidase, α-mannosidase, and trypsin. Important dual virulence factors found in ...
Alpha-fucosidase may refer to one of two enzymes: Fucosidase Alpha-L-fucosidase This set index page lists enzyme articles ...
alpha-L-fucosidase 2. involved_in. IEA. Ensembl. GO_REF:0000107. NCBI chrNW_004936625:2,636,136...2,653,328 Ensembl chrNW_ ... integrin subunit alpha V. involved_in. IEA. Ensembl. GO_REF:0000107. NCBI chrNW_004936506:10,750,116...10,839,018 Ensembl chrNW ...
The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. This enzyme plays a role in the breakdown ... FUCA1 gene mutations severely reduce or eliminate the activity of the alpha-L-fucosidase enzyme. A lack of enzyme activity ... Alpha-L-fucosidase is responsible for cutting (cleaving) off a sugar molecule called fucose toward the end of the breakdown ...
2-naphthyl-alphaL-fucopyranosidealpha- Fucosidase [Ref.: #19706]. 531. not determinedn.d. + + + - + - - - - + + - - - + + - - ... alpha-Glucosidasealpha GLU N-Acetyl-beta-Glucosidasebeta NAG Esculin hydrolysis/beta-GlucosidaseESC Urease/urea hydrolysisURE ... 1-O-methyl-alpha-D-glucoside as carbon sourceMDG 3-O-methyl-D-glucose as carbon source3MDG D-saccharate as carbon sourceSAT ... 1-O-methyl-alpha-galactopyranoside as carbon sourceMaGa D-cellobiose as carbon sourceCEL gentiobiose as carbon sourceGEN 1-O- ...
Alpha-fucosidase. * Fabry disease. Alpha-galactosidase. *Schindler/Kanzaki disease. Alpha-N-acetylgalactosaminidase ...
alpha-L-Fucosidase [D08.811.277.450.050] alpha-L-Fucosidase * Amylases [D08.811.277.450.066] ...
Alpha-L-Fucosidase. UREA. Urea. P. Phosphorus. FMN. Flavin Mono Nucleotide. CREA. Creatinine. C. Carbon. HDL-C. High Density ... alpha-hydroxy butyrate dehydrogenase. PA. AST/GOT. Aspartate Aminotransferase/. Serum glutamic-oxaloacetic transaminase. AMY. ...
Alpha-N-acetylgalactosaminidase; Alpha-galactosidase; Beta-galactosidase; ... Methodology includes Fluorometry. ... Deficiency of alpha-mannosidase; Fabry disease; ... Testing proteins (4): Glycogen debranching enzyme; Heparan Sulphamidase; N- ... Glycogen debranching enzyme; Heparan Sulphamidase; N-Neuraminidase; Plasma alpha-L-fucosidase Methods (1): Help ... Alpha-N-acetylgalactosaminidase; Alpha-galactosidase; Beta-galactosidase; Beta-glucocerebrosidase; Beta-hexosaminidase subunit ...
FUCOSIDASE. ALPHA-L-FUCOSIDASE. GALACTOSEMIA. GALACTOSEMIAS. GANGLIOSIDOSIS G(M1). GANGLIOSIDOSIS GM1. GAUCHERS DISEASE. ...
FUCOSIDASE. ALPHA-L-FUCOSIDASE. GALACTOSEMIA. GALACTOSEMIAS. GANGLIOSIDOSIS G(M1). GANGLIOSIDOSIS GM1. GAUCHERS DISEASE. ...
Low levels of alpha-L-fucosidase can be detected in plasma, urine, and leukocytes. Glycolipids and glycoproteins have also been ... lysosomal storage disease in which fucose accumulates in tissue as a result of defective alpha-L-fucosidase. The responsible ...
... including L-fucosidase, beta-mannosidase, neuramidase, beta-galactosidase, and alpha-N-acetylgalactosaminidase. In addition, ... Scott M Acker, MD is a member of the following medical societies: Alpha Omega Alpha, American Medical Association, American ... Broad range of adverse cutaneous eruptions in patients on TNF-alpha antagonists. J Cutan Pathol. 2012 May. 39(5):481-92. [QxMD ... It is usually associated with Anderson-Fabry disease, an X-linked recessive disorder characterized by a deficiency of alpha- ...
K15923 alpha-L-fucosidase 2 [EC:3.2.1.51] K01216 licheninase [EC:3.2.1.73] K20830 beta-porphyranase [EC:3.2.1.178] COG2273 Beta ... K01176 alpha-amylase [EC:3.2.1.1] K05343 maltose alpha-D-glucosyltransferase / alpha-amylase [EC:5.4.99.16 3.2.1.1] K05992 ... maltogenic alpha-amylase / neopullulanase [EC:3.2.1.54 3.2.1.133 3.2.1.135] COG0366 Glycosidase K06113 arabinan endo-1,5-alpha- ... As you can see, we found 2 annotations for the sialidase, 2 for the fucosidase, 6 for the β-galactosidase, 1 for the α-amylase ...
... alpha-L-fucosidase - metabolism ; Alpha-Mannosidase - metabolism ; alpha-L-fucosidase - urine ; beta-Galactosidase - metabolism ... Tytu orygina u: The activity of alpha-mannosidase and alpha fucosidase in liver cancerous tissue.. Czasopismo: Experimental & ... alpha-L-fucosidase - metabolism ; Alpha-Mannosidase - metabolism ; beta-Galactosidase - metabolism. Charakt. formalna: Polski ... Alpha-Mannosidase - metabolism ; beta-Galactosidase - metabolism ; alpha-L-fucosidase - metabolism. Charakt. formalna: Polski ...
A second lysosomal enzyme, alpha-fucosidase, was strongly inhibited by DAB treatment with the residual activity corresponding ... Hexosaminidases/metabolismo , Lisossomos/enzimologia , Peroxidases/metabolismo , alfa-L-Fucosidase/metabolismo , Animais , ...
... and structural biology indicate that the encoded cohort of an alpha-xylosidase, a beta-galactosidase, and an alpha-l-fucosidase ...
alpha-L-Fucosidase. *Amylases. *beta-Fructofuranosidase. *Chitinase. *Dextranase. *Disaccharidases. *Galactosidases. * ...
... including L-fucosidase, beta-mannosidase, neuramidase, beta-galactosidase, and alpha-N-acetylgalactosaminidase. In addition, ... Scott M Acker, MD is a member of the following medical societies: Alpha Omega Alpha, American Medical Association, American ... Broad range of adverse cutaneous eruptions in patients on TNF-alpha antagonists. J Cutan Pathol. 2012 May. 39(5):481-92. [QxMD ... It is usually associated with Anderson-Fabry disease, an X-linked recessive disorder characterized by a deficiency of alpha- ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Lysophosphatidic acid acyltransferase alpha,1-AGP acyltransferase 11,Acetyl-CoA:lyso-PAF acetyltransferase,LPAAT-alpha ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Human HNF1a(Hepatocyte Nuclear Factor 1 Alpha) ELISA Kit. *Human HSD17b1(17-Beta-Hydroxysteroid Dehydrogenase Type 1) ELISA Kit ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Human HNF1a(Hepatocyte Nuclear Factor 1 Alpha) ELISA Kit. *Human HSD17b1(17-Beta-Hydroxysteroid Dehydrogenase Type 1) ELISA Kit ... Human HIF1aN(Hypoxia Inducible Factor 1 Alpha Subunit Inhibitor) ELISA Kit. *Human HIP2(Huntingtin Interacting Protein 2) ELISA ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Human HIF1aN(Hypoxia Inducible Factor 1 Alpha Subunit Inhibitor) ELISA Kit. *Human HIP2(Huntingtin Interacting Protein 2) ELISA ... Human PI4Ka(Phosphatidylinositol-4-Kinase Catalytic Alpha) ELISA Kit. *Human PIAS3(Protein Inhibitor Of Activated STAT 3) ELISA ...
Human FUCa1(Fucosidase Alpha L1, Tissue) ELISA Kit. *Human GAL1(Galectin 1) ELISA Kit ... Human MIP3a(Macrophage Inflammatory Protein 3 Alpha) ELISA Kit. *Human MIP4a(Macrophage Inflammatory Protein 4 Alpha) ELISA Kit ... Human TNFa(Tumor Necrosis Factor Alpha) ELISA Kit. *Human TNFRSF1A(Tumor Necrosis Factor Receptor Superfamily, Member 1A) ELISA ... Mouse TNFa(Tumor Necrosis Factor Alpha) ELISA Kit. *Mouse TNFRSF5(Tumor Necrosis Factor Receptor Superfamily, Member 5) ELISA ...
Human FUCa1(Fucosidase Alpha L1, Tissue) ELISA Kit. *Human TPO(Thyroid Peroxidase) ELISA Kit ... Human MIP1a(Macrophage Inflammatory Protein 1 Alpha) ELISA Kit. *Mouse MIP1a(Macrophage Inflammatory Protein 1 Alpha) ELISA Kit ... Human MIP3a(Macrophage Inflammatory Protein 3 Alpha) ELISA Kit. *Mouse MIP3a(Macrophage Inflammatory Protein 3 Alpha) ELISA Kit ... Human ITaC(Interferon Inducible T-Cell Alpha Chemoattractant) ELISA Kit. *Mouse ITaC(Interferon Inducible T-Cell Alpha ...
α-(1-6) Fucosidase. α-(1-3,4) Fucosidase. Ludger α-(1-3,4) Fucosidase. Glycan Sequencing Kit ... The specificity of viral and bacterial sialidases for alpha(2-3) and alpha(2-6)-linked sialic acids in glycoproteins. Biochim ... Sialidase, N-acetylneuraminate glycohydrolase, Exo-alpha-sialidase. α(2-3) Neuraminidase Sp cleaves exclusively the non- ... Specifictity Cleaves the non-reducing terminal alpha-(2-3) unbranched sialic acid residues from complex carbohydrates and ...
Alpha L fucosidase deficiency.. *Fucosidosis type III. Alpha L fucosidase deficiency.. *Fukuyama congenital muscular dystrophy. ... Alpha-mannosidosis type I. Infantile variety. Alpha-d-mannosidase deficiency.. *Alpha-mannosidosis type II. Juvenile form. ... Alpha-Ketoglutaric aciduria. Alpha-ketoglutaric acid dehydrogenase deficiency.. 3 (Back to top). *3-Hydroxy-3-methyl glutaryl- ... Fucosidosis type I. Alpha L fucosidase deficiency.. *Fucosidosis type II. ...
Alpha-L-fucosidase deficiency. Inheritance type Autosomal recessive. Prevalence *Worldwide: ,1 in 1,000 000 ...
  • Alpha-fucosidase may refer to one of two enzymes: Fucosidase Alpha-L-fucosidase This set index page lists enzyme articles associated with the same name. (wikipedia.org)
  • The FUCA1 gene provides instructions for making an enzyme called alpha-L-fucosidase. (medlineplus.gov)
  • FUCA1 gene mutations severely reduce or eliminate the activity of the alpha-L-fucosidase enzyme. (medlineplus.gov)
  • In harness, transcriptomics, reverse genetics, enzyme kinetics, and structural biology indicate that the encoded cohort of an alpha-xylosidase, a beta-galactosidase, and an alpha-l-fucosidase is specifically adapted for efficient, concerted saccharification of dicot (fucogalacto) xyloglucan oligosaccharides following import into the periplasm via an associated TonB-dependent receptor. (unl.edu)
  • Specific Activity Defined as the amount of enzyme required to produce 1 µmole of methylumbelliferone in 1 minute at 37˚C, pH 5.0 from MU-NANA [2′-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid]. (qa-bio.com)
  • Specifictity Cleaves the non-reducing terminal alpha-(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins. (qa-bio.com)
  • The specificity of viral and bacterial sialidases for alpha(2-3) and alpha(2-6)-linked sialic acids in glycoproteins. (qa-bio.com)
  • Low levels of alpha-L-fucosidase can be detected in plasma, urine, and leukocytes. (arizona.edu)
  • Alpha-L-fucosidase is responsible for cutting (cleaving) off a sugar molecule called fucose toward the end of the breakdown process. (medlineplus.gov)
  • The aim of this work was to extend the knowledge about tissue alpha-L-fucosidase in colorectal cancer by quantifying the expression of its encoding gene FUCA1 in tumors and healthy mucosa. (nih.gov)
  • Our results demonstrated diminished FUCA1 mRNA levels in tumors, suggesting that expression of tissue alpha-L-fucosidase could be regulated at transcriptional level in colorectal cancer. (nih.gov)
  • Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. (nih.gov)
  • In previous studies we described a decreased alpha-L-fucosidase activity in colorectal tumors, appearing as a prognostic factor of tumoral recurrence. (nih.gov)
  • 14. Alpha-1-fucosidase as a prognostic indicator for hepatocellular carcinoma following hepatectomy: a large-scale, long-term study. (nih.gov)
  • Alpha-L-fucosidase is responsible for cutting (cleaving) off a sugar molecule called fucose toward the end of the breakdown process. (medlineplus.gov)
  • Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. (nih.gov)
  • Lactobacillus casei produces an α-fucosidase, called AlfC, with specificity towards α(1,6)-fucose, the only linkage found in human N-glycan core fucosylation. (bvsalud.org)
  • 16. [A preliminary study on serum alpha-L-fucosidase assay in the diagnosis of hepatocellular carcinoma]. (nih.gov)
  • 6. Serum midkine is a more sensitive predictor for hepatocellular carcinoma than Dickkopf-1 and alpha-L-fucosidase in cirrhotic HCV patients. (nih.gov)
  • 7. Alpha-L-fucosidase as a serum marker of hepatocellular carcinoma in Thailand. (nih.gov)
  • 13. A comparison of glypican-3 with alpha-fetoprotein as a serum marker for hepatocellular carcinoma: a meta-analysis. (nih.gov)
  • 18. [Value of the serum measurement of alpha-L-fucosidase in the diagnosis of hepatocarcinoma]. (nih.gov)
  • 19. Serum alpha-L-fucosidase. (nih.gov)
  • 20. [Diagnostic significance of the determination of serum alpha-L-fucosidase in primary hepatocellular carcinoma]. (nih.gov)
  • Serum alpha fetoprotein (AFP) is the most widely used tumor marker in detecting patients with hepatocellular carcinoma, and has been proven to have capability of prefiguring the prognosis. (nih.gov)
  • 4. Clinical performance of α-L-fucosidase for early detection of hepatocellular carcinoma. (nih.gov)
  • While alpha-fetoprotein (AFP) is a commonly used tumor marker in the detection of hepatocellular carcinoma (HCC), its sensitivity and specificity are insufficient to detect HCC in all patient samples. (medscape.com)
  • Furthermore, some other tumor markers, such as glypican-3, gamma-glutamyl transferase II, alpha-l-fucosidase, transforming growth factor-beta1, tumor-specific growth factor, have been indicated to be available supplementaries to AFP in the detection. (nih.gov)
  • 10. Golgi protein 73 versus alpha-fetoprotein as a biomarker for hepatocellular carcinoma: a diagnostic meta-analysis. (nih.gov)
  • In addition, activity and expression of alpha-L-fucosidase in selected matched tumor and healthy mucosa samples were analyzed. (nih.gov)