GALE

Last update 23 Jan 2025

Basic Info

Synonyms

Galactowaldenase, GALE, SDR1E1

+ [7]

Introduction

Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.

100 Clinical Results associated with GALE

100 Translational Medicine associated with GALE

0 Patents (Medical) associated with GALE

1,045

Literatures (Medical) associated with GALE

01 Mar 2025·Gene

Analyses of biosynthesis mutants reveal that the fifth and sixth sugars of the Porphyromonas gingivalis O-glycan are L-fucose and N-acetylgalactosamine respectively

Article

Author: Shoji, Mikio ; Veith, Paul D ; Reynolds, Eric C

The oral pathogen, Porphyromonas gingivalis has a general O-glycosylation system which it utilises to modify hundreds of proteins localised outside of the cytoplasm. The O-glycan is a heptasaccharide that includes a putative L-fucose and N-acetylgalactosamine (GalNAc) as the 5th and 6th sugar residues respectively. The putative L-fucose is expected to be synthesized as GDP-L-fucose involving the enzymes Gmd (PGN_1078) and Fcl (PGN_1079), while GalNAc is putatively epimerised from GlcNAc by GalE (PGN_1614). In this study we created mutants lacking each of these three enzymes and analysed the resultant glycosylation defects. Immunoblot analysis using antibodies against the model glycoproteins Mfa2, PGN_0742 and PGN_1037 detected bands of reduced size, consistent with glycan truncation. Mass spectrometry analysis of tryptic digests of whole cell lysate proteins revealed that O-glycans in the galE mutant were predominantly pentasaccharides consistent with the 6th sugar being GalNAc. For the gmd and fcl mutants, tetrasaccharides were observed confirming the 5th sugar as L-fucose. The confirmation of these sugars also confirmed PGN_1135 as a GalNAc transferase as the previously analysed PGN_1135 mutant produced the same O-glycan truncation as the galE mutant.

01 Feb 2025·Food Chemistry

Regional and longitudinal dynamics of human milk protein components assessed by proteome analysis on a fast and robust micro-flow LC–MS/MS system

Article

Author: Li, Hongmei ; Jiang, Shilong ; Zhen, Kemiao ; Wang, Hui ; Wei, Qiaosi ; Ma, Wen ; Cao, Junxia ; Ying, Wantao ; Cui, Xinling ; Lu, Hai ; Yue, Zhan

An in-depth exploration of molecular composition of human milk could provide a scientific basis for the development of substitutes. The present study was conducted to analyze human milk proteins from 110 individuals from five regions of China and across three stages of lactation to investigate the change patterns. We developed a micro-flow liquid chromatography tandem mass spectrometry (μLC-MS/MS) system with data-independent acquisition (DIA) proteomics technology that can rapidly and stably characterize the human milk proteome. In total, 2796 proteins were identified. Among these proteins, CPM, ACSL1, and RPL13 changed significantly during lactation, and SCP2, GALK1 and GALE changed significantly between regions. Bioinformatics analysis revealed that human milk is altered by complex interactions between genetic and environmental factors. Our results not only reveal the regional and longitudinal patterns of change in human milk proteome but also provide theoretical basis and technical support for the production and quality control of infant formula.

15 Jan 2025·Journal of Agricultural and Food Chemistry

Thermostability Enhancement of Tagatose 4-Epimerase through Protein Engineering and Whole-Cell Immobilization

Article

Author: Guo, Xuehong ; Liu, Zhanzhi ; Wu, Jing ; Xu, Ying

d-Tagatose, a rare sugar endowed with a low-calorie property, superior taste quality, and probiotic functionality, has garnered significant research attention. However, the prevailing biological production methods relying on β-galactosidase and l-arabinose isomerase face challenges including high cost and suboptimal conversion efficiency. Consequently, it is of great research significance to find efficient alternative routes for d-tagatose synthesis. Previously, Thermotoga petrophila tagaturonate 3-epimerase was modified to function as tagatose 4-epimerase (T4E) enabling the direct conversion of d-fructose to d-tagatose. In this study, T4E was further engineered through directed evolution, specifically targeting the enhancement of its thermostability for application. This endeavor yielded promising T4E variants with superiority over those of the original enzyme. T4E I430P exhibits a half-life (t_1/2) at 70 °C that is 1.83-fold that of T4E, with an increased melting temperature (T_m) of 5.1 °C compared to T4E. Additionally, T4E G90S/T272A/I430P demonstrated a 21.4% increase in specific activity compared to T4E. At 70 °C, its t_1/2 was 1.69-fold that of T4E, and its T_m is 2.9 °C higher than T4E. Furthermore, whole-cell immobilization integrating these engineered T4E variants into a robust biocatalytic system was employed. This innovative approach not only underscores the practical feasibility of modifying enzymes through directed evolution but also establishes a foundation for the cost-effective, large-scale production of d-tagatose.

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