FPGT

Last update 08 May 2025

Basic Info

Synonyms

FPGT, fucose-1-phosphate guanylyltransferase, GDP-L-fucose diphosphorylase

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Introduction

Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate (PubMed:9804772). Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids (PubMed:9804772).

100 Clinical Results associated with FPGT

100 Translational Medicine associated with FPGT

0 Patents (Medical) associated with FPGT

Literatures (Medical) associated with FPGT

01 Apr 2025·Journal of Biological Chemistry

Structural insight into the catalytic mechanism of the bifunctional enzyme l-fucokinase/GDP-fucose pyrophosphorylase

Article

Author: Lin, Chun-Hung ; Chiang, Hung-Yu ; Wu, Cheng-Guo ; Wang, Andrew H-J ; Hsu, Min-Feng ; Ko, Tzu-Ping ; Lin, Sheng-Wei

The bifunctional l-fucokinase/GDP-β-l-fucose pyrophosphorylase (FKP) from Bacteroides fragilis catalyzes the conversion from l-fucose to GDP-β-l-fucose. The reaction product, representing the activated form of l-fucose, is used by all l-fucosyltransferases to incorporate l-fucose. Herein, we report the first X-ray crystal structures of FKP in complex with substrate-product, leading to the dissection of both activity domains and corresponding catalytic mechanisms. The full-length FKP (FKP-FL, 949 amino acids) exists as a tetramer in solution, but the individually prepared N-terminal domain (FKP-NTD corresponding to the sequence 1-496, also containing a SUMO tag) and C-terminal domain (FKP-CTD, the sequence 519-949) form a monomer and a dimer, respectively. FKP-NTD has a single α/β domain and a β-helix-containing domain, whereas FKP-CTD folds into two α/β domains and the linker comprises three α-helices. The β-l-fucose-1-phosphate (fucose-1-P) and GTP bound separately to the active sites of fucokinase (located at FKP-CTD) and pyrophosphorylase (FKP-NTD), and a third nucleotide-binding site is adjacent to the β-helix (also in FKP-NTD). Furthermore, Asp762 was proposed to serve as the general base in the reaction of fucokinase, to deprotonate the C1-OH of fucose in the nucleophilic attack to γ-phosphate of ATP, resulting in the formation of fucose-1-P. At the same time, Arg592 and magnesium ion stabilize the developing negative charge in the leaving group (ADP). Subsequently, in the pyrophosphorylase-catalyzed reaction, the Lys187 side chain facilitates the nucleophilic attack of fucose-1-P toward GTP, leading to the formation of GDP-fucose.

01 Oct 2024·Veterinary Parasitology

Analysis of potential genes, immunological and antioxidant profiles associated with trypanosomiasis susceptibility in dromedary camels

Article

Author: Barghash, Safaa M ; Ateya, Ahmed I ; Wassif, Islam M ; Elsayed, Ahmed A ; Osman, Wafaa A ; El-Kattan, Adel M

Trypanosomiasis is associated with tissue damage and may trigger an immunological response. These tissue lesions are linked to metabolic issues and oxidative stress. The current study aimed to investigate the immunological, antioxidant, and metabolic changes that may be connected to camel trypanosomiasis. Blood samples were collected from 54 camels and allocated into two groups: The control group (35 camels) and the infected group (19 camels). The genes TLR2, TLR5, IL-17, MARCHF3, RASGRP1, EPS15L1, PPIE, ASB16, CMPK2, LPCAT1, FPGT, GPHN, TNNI3K, DIO3, keap1, and OXSR1 were significantly up-regulated in trypanosomiasis camels. However, down-regulation was observed for the genes Nrf2, PRDX6, and NDUFS5. PCR-DNA sequencing was used to identify nucleotide sequence polymorphisms in the immune (TLR2, TLR5, IL-17, MARCHF3, RASGRP1, and EPS15L1), metabolic (PPIE, ASB16, CMPK2, LPCAT1, FPGT, GPHN, TNNI3K, and DIO3), and antioxidant (Nrf2, Keap1, PRDX6, NDUFS5, and OXSR1) genes between healthy and trypanosomiasis-affected camels. Exploring the serum profile also showed a significant (P ˂ 0.05) increase in Hp, SAA, Cp, IL-1β, IL-6, IL 10, TNF-α, and MDA, with significant (P ˂ 0.05) reduction in the serum levels of CAT, SOD, GSH, T3, and T4 in diseased camels compared with healthy ones. Our findings confirm the significance of nucleotide variations, gene expression patterns, and the biochemical profile of the investigated markers as indicators for the susceptibility of trypanosomiasis in dromedary camels and may be utilized to create management strategies.

27 Nov 2023·Angewandte Chemie International Edition

Subrutilane—A Hexacyclic Sesterterpene from Streptomyces subrutilus

Article

Author: Goldfuss, Bernd ; Schnakenburg, Gregor ; Gu, Binbin ; Dickschat, Jeroen S

AbstractMining of a terpene synthase from Streptomyces subrutilus resulted in the identification of the hexacyclic sesterterpene subrutilane, besides eight pentacyclic side products. Subrutilane represents the first case of a saturated sesterterpene hydrocarbon. Its structure, including the absolute configuration, was unambiguously determined through X‐ray crystallographic analysis and stereoselective deuteration. The cyclisation mechanism to subrutilane and its side products was investigated in all detail by isotopic labelling experiments and DFT calculations. The subrutilane synthase (SrS) also converted (2Z)‐GFPP into one major product. Additional compounds were obtained from the substrate analogues (7R)‐6,7‐dihydro‐GFPP and (2Z,7R)‐6,7‐dihydro‐GFPP with blocked reactivity at the C6−C7 bond. Interestingly, the early steps of the cyclisation cascade with (2Z)‐GFPP and the saturated substrate analogues were analogous to those of GFPP, but then deviations from the natural cyclisation mode occur.

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FPGT

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