ArticleJournal of molecular biology2007
Role of a single amino acid in the evolution of glycans of invertebrates and vertebrates.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Comparative Silk Transcriptomics Illuminates Distinctive Impact of Artificial Selection in Silkworm Modern Breeding.Insects · 2022Article
- Bombyx mori β1,4-N-acetylgalactosaminyltransferase possesses relaxed donor substrate specificity in N-glycan synthesis.Scientific reports · 2021Article
- Aberration of Serum and Tissue N-Glycans in Mouse β1,4-GalT1 Y286L Mutant Variants.Glycoconjugate journal · 2020Article
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- Article
- Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016Review
- Genetic, biochemical, and serological characterization of a new pneumococcal serotype, 6H, and generation of a pneumococcal strain producing three different capsular repeat units.Clinical and vaccine immunology : CVI · 2015Article
- Discovery of Streptococcus pneumoniae serotype 6 variants with glycosyltransferases synthesizing two differing repeating units.The Journal of biological chemistry · 2013Article
- Streptococcus pneumoniae serotype 11D has a bispecific glycosyltransferase and expresses two different capsular polysaccharide repeating units.The Journal of biological chemistry · 2013Article
- The N's and O's of Drosophila glycoprotein glycobiology.Glycoconjugate journal · 2013Review
- A single point mutation in the gene encoding Gb3/CD77 synthase causes a rare inherited polyagglutination syndrome.The Journal of biological chemistry · 2012Article
- Binding of N-acetylglucosamine (GlcNAc) β1-6-branched oligosaccharide acceptors to β4-galactosyltransferase I reveals a new ligand binding mode.The Journal of biological chemistry · 2012Article
- Genetic Interactions Between Drosophila sialyltransferase and β1,4-N-acetylgalactosaminyltransferase-A Genes Indicate Their Involvement in the Same Pathway.G3 (Bethesda, Md.) · 2012Article
- Structure-based evolutionary relationship of glycosyltransferases: a case study of vertebrate β1,4-galactosyltransferase, invertebrate β1,4-N-acetylgalactosaminyltransferase and α-polypeptidyl-N-acetylgalactosaminyltransferase.Current opinion in structural biology · 2010Review
- Structure and function of beta -1,4-galactosyltransferase.Current drug targets · 2008Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Structures of glycoconjugate N-glycans and glycolipids of invertebrates show significant differences from those of vertebrates. These differences are due largely to the vertebrate beta1,4-galactosyltransferase-1 (beta4Gal-T1), which is found as a beta1,4-N-acetylgalactosaminyltransferase (beta4GalNAc-T1) in invertebrates. Mutation of Tyr285 to Ile or Leu in human beta4Gal-T1 converts the enzyme into an equally efficient beta4GalNAc-T1. A comparison of all the human beta4Gal-T1 ortholog enzymes shows that this Tyr285 residue in human beta4Gal-T1 is conserved either as Tyr or Phe in all vertebrate enzymes, while in all invertebrate enzymes it is conserved as an Ile or Leu. We find that mutation of the corresponding Ile residue to Tyr in Drosophila beta4GalNAc-T1 converts the enzyme to a beta4Gal-T1 by reducing its N-acetylgalactosaminyltransferase activity by nearly 1000-fold, while enhancing its galactosyltransferase activity by 80-fold. Furthermore, we find that, similar to the vertebrate/mammalian beta4Gal-T1 enzymes, the wild-type Drosophila beta4GalNAc-T1 enzyme binds to a mammary gland-specific protein, alpha-lactalbumin (alpha-LA). Thus, it would seem that, during the evolution of vertebrates from invertebrates over 500 million years ago, beta4Gal-T1 appeared as a result of the single amino acid substitution of Tyr or Phe for Leu or Ile in the invertebrate beta4GalNAc-T1. Subsequently, the pre-existing alpha-LA-binding site was utilized during mammalian evolution to synthesize lactose in the mammary gland during lactation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.