Identification of Key Functional Residues in the Active Site of Human β1,4-Galactosyltransferase 7
Open accessAbstract
Glycosaminoglycans (GAGs) play a central role in many pathophysiological events, and exogenous xyloside substrates of β1,4-galactosyltransferase 7 (β4GalT7), a major enzyme of GAG biosynthesis, have interesting biomedical applications. To predict functional peptide regions important for substrate binding and activity of human β4GalT7, we conducted a phylogenetic analysis of the β1,4-galactosyltransferase family and generated a molecular model using the x-ray structure of Drosophila β4GalT7-UDP as template. Two evolutionary conserved motifs, (163)DVD(165) and (221)FWGWGREDDE(230), are central in the organization of the enzyme active site. This model was challenged by systematic engineering of point mutations, combined with in vitro and ex vivo functional assays. Investigation of the kinetic properties of purified recombinant wild-type β4GalT7 and selected mutants identified Trp(224) as a key residue governing both donor and acceptor substrate binding. Our results also suggested the involvement of the canonical carboxylate residue Asp(228) acting as general base in the reaction catalyzed by human β4GalT7. Importantly, ex vivo functional tests demonstrated that regulation of GAG synthesis is highly responsive to modification of these key active site amino acids. Interestingly, engineering mutants at position 224 allowed us to modify the affinity and to modulate the specificity of human β4GalT7 toward UDP-sugars and xyloside acceptors. Furthermore, the W224H mutant was able to sustain decorin GAG chain substitution but not GAG synthesis from exogenously added xyloside. Altogether, this study provides novel insight into human β4GalT7 active site functional domains, allowing manipulation of this enzyme critical for the regulation of GAG synthesis. A better understanding of the mechanism underlying GAG assembly paves the way toward GAG-based therapeutics.
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Biochemical methods to assess GAG synthesis in patients' cultured fibroblasts are currently available in many specialized laboratories.
“For definite proof of GAG deficiency ( B4GALT7 and B3GALT6 mutations), biochemical methods to assess GAG synthesis in patients ' cultured fibroblasts are currently available in many specialized laboratories [Talhaoui et al., 2010].”
From The 2017 international classification of the Ehlers–Danlos syndromes (2017) · cites this paper as Talhaoui et al., 2010
The “Analysis of GAG Synthesis by Na₂[³⁵S]SO₄ Incorporation” methods section describes a biochemical assay for GAG synthesis, and the methods text on p. 37345 describes measuring total GAG synthesis. Both use cultured CHO cells, not patients’ fibroblasts; the paper does not establish that such testing is available in many specialized laboratories or that it provides definite proof of deficiency from both B4GALT7 and B3GALT6 mutations. (LLM, conf=0.88)
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- Authors
- Talhaoui, I., Bui, C., Oriol, R., Mulliert, G., Gulberti, S., Netter, P., Coughtrie, M. W. H., Ouzzine, M., & Fournel-Gigleux, S.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Dundee (GB)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 285
- Issue
- 48
- Pages
- 37342-37358
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2988340
- OpenAlex
- W1987627048
- Cited by
- 26
- References
- 51
- Citations by year
- 2026: 2 · 2024: 2 · 2021: 3 · 2020: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 1 · 2013: 4 · 2012: 2
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (publishedVersion)
- HAL (submittedVersion, cc-by)
- Newcastle University ePrints (Newcastle Univesity)
- Funders
- University of Dundee
- Agence Nationale de la Recherche (ANR-08-PCVI-0023)
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- glycosaminoglycan synthesis, active site residues, enzyme kinetic properties, decorin, phylogenetic analysis
- MeSH terms
- Amino Acid Sequence, Animals, Galactosyltransferases, Glycosaminoglycans, Humans, Invertebrates, Models, Molecular, Molecular Sequence Data, Phylogeny, Substrate Specificity, Vertebrates, Sequence Alignment, Catalytic Domain, Amino Acid Motifs
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