Last update 01 Nov 2024

FUCA1

Last update 01 Nov 2024

Basic Info

Synonyms

alpha-L-fucosidase 1, Alpha-L-fucosidase I, Alpha-L-fucoside fucohydrolase 1

+ [2]

Introduction

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.

Drugs associated with FUCA1

CN115850496

Patent Mining

Target

FUCA1

Mechanism-

Active Org.

Shandong Naruiborn Biomedical Technology Co., Ltd.

Originator Org.

Shandong Naruiborn Biomedical Technology Co., Ltd.

Active Indication

Neoplasms [+1]

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

GRI-2

Target

FUCA1

Mechanism

FUCA1 modulators

Active Org.-

Originator Org.

Allelix Neuroscience, Inc.

Active Indication-

Inactive Indication

Muscle Hypertonia

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with FUCA1

100 Translational Medicine associated with FUCA1

0 Patents (Medical) associated with FUCA1

1,073

Literatures (Medical) associated with FUCA1

01 Nov 2024·Gene

Potential predictive value of immune-related genes FUCA1 and NCKAP1L for osteosarcoma metastasis

Article

Author: Dou, Junzhe ; Liu, Maorong ; Tong, Zhichao ; Zhang, Yunheng ; Wang, Xuan ; Li, Yi

BACKGROUNDOsteosarcoma is a common malignant tumor with a low survival rate after metastasis. Current treatments have not proven to effectively increase patient survival rates. Immunotherapy is a promising new treatment approach, however, immune target therapy has not shown satisfactory results. This study aims to provide new insights and evidence for the use of immunotherapy in osteosarcoma, based on a comprehensive analysis of gene expression data from databases.METHODSGene expression and GSAV analysis were conducted on samples from patients with metastatic and non-metastatic osteosarcoma in the TARGET and GEO databases to identify relevant genes. These genes were further analyzed using GO, KEGG, GSVA, correlation analysis, and immune microenvironment scoring techniques. The tissue location of gene expression was confirmed through single-cell analysis. Validation of gene expression patterns was performed using polymerase chain reaction, western blot, and immunohistochemistry.RESULTSThe study identified FUCA1 and NCKAP1L as significantly enriched in non-metastatic osteosarcoma, with higher expression associated with better patient survival rates. Gene function enrichment was primarily related to immune functions, with positive correlations to macrophage phagocytosis, antigen presentation, and macrophage polarization pathways. Analysis of the immune microenvironment revealed a positive correlation between gene expression and immune scores, with increased presence of macrophages, T cells, and B cells in the high expression group. Single-cell analysis and experimental results confirmed the enrichment of FUCA1 and NCKAP1L in macrophages.CONCLUSIONThe identification of FUCA1 and NCKAP1L as potential prognostic biomarkers suggests their potential for improving patient outcomes. Modulation of macrophages may offer a promising strategy for enhancing the immune microenvironment in osteosarcoma.

01 Nov 2024·Carbohydrate Research

Purification and characterization of α-fucosidase from Dichostereum sordulentum 1488

Article

Author: Herrera, Lorena ; Bonnecarrere, Paula Rodríguez ; Giacomini, Cecilia ; Rodríguez Bonnecarrere, Paula ; Cedrés, María Eugenia

Biological glycans mediate several physiological processes, thus altered glycosylation patterns can lead to different diseases such as autoimmune, infectious, chronic anti-inflammatory diseases, or even cancer. In fact, alterations in fucosylation in either N- or O-glycans are among the most frequent changes in glycosylation patterns associated with cancer. Therefore, elucidation of the role of glycoconjugate glycans is essential for understanding the development of pathologies where they are involved. In this sense glycosidases are excellent tools, since they catalyse the selective removal of sugar residues, allowing the evaluation of changes in their biological role due to glycan removal. This work describes the purification and characterization of a α-fucosidase from the fungus Dichostereum sordulentum 1488. It is a homodimer with a molecular weight of 214 kDa and optimum pH and temperature of 4.0 and 70 °C respectively. It has a K_M of 0.27 mM and V_Max of 3.3 μmoles PNP/min per mg for the substrate p-nitrophenyl-α-l-fucopyranoside, showing a substrate inhibition profile. It showed high specificity for the hydrolysis of fucose linked by α-(1,2) bonds. The identification, purification, and characterization of this new α-fucosidase is highly relevant for enlarging the availability of glycosidases for use as tools for glycan elucidation.

01 Oct 2024·Journal of the Science of Food and Agriculture

Characterization of an α‐L‐fucosidase in marine bacterium Wenyingzhuangia fucanilytica: new evidence on the catalytic sites of GH95 family glycosidases

Article

Author: Mei, Xuanwei ; Zhang, Yuying ; Xue, Changhu ; Shen, Jingjing ; Chang, Yaoguang ; Li, Jiajing

AbstractBackgroundα‐l‐Fucose confers unique functions for fucose‐containing biomolecules such as human milk oligosaccharides. α‐l‐Fucosidases can serve as desirable tools in the application of fucosylated saccharides. Discovering novel α‐l‐fucosidases and elucidating their enzyme properties are always worthy tasks.ResultsA GH95 family α‐l‐fucosidase named Afc95A_Wf was cloned from the genome of the marine bacterium Wenyingzhuangia fucanilytica and expressed in Escherichia coli. It exhibited maximum activity at 40 °C and pH 7.5. Afc95A_Wf defined a different substrate specificity among reported α‐l‐fucosidases, which was capable of hydrolyzing α‐fucoside in CNP‐fucose, Fucα1‐2Galβ1‐4Glc and Galβ1‐4(Fucα1‐3)Glc, and showed a preference for α1,2‐fucosidic linkage. It adopted Asp residue in the amino acid sequence at position 391, which was distinct from the previously acknowledged residue of Asn. The predicted tertiary structure and site‐directed mutagenesis revealed that Asp391 participates in the catalysis of Afc95A_Wf. The differences in the substrate specificity and catalytic site shed light on that Afc95A_Wf adopted a novel mechanism in catalysis.ConclusionA GH95 family α‐l‐fucosidase (Afc95A_Wf) was cloned and expressed. It showed a cleavage preference for α1,2‐fucosidic linkage to α1,3‐fucosidic linkage. Afc95A_Wf demonstrated a different substrate specificity and a residue at an important catalytic site compared with known GH95 family proteins, which revealed the occurrence of diversity on catalytic mechanisms in the GH95 family. © 2024 Society of Chemical Industry.

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FUCA1

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