Acceptor substrate binding revealed by crystal structure of human glucosamine‐6‐phosphate N‐acetyltransferase 1

@article{Wang2008AcceptorSB,
  title={Acceptor substrate binding revealed by crystal structure of human glucosamine‐6‐phosphate N‐acetyltransferase 1},
  author={Juan Wang and Xiang Liu and Yu-He Liang and Lan-fen Li and Xiao-Dong Su},
  journal={FEBS Letters},
  year={2008},
  volume={582}
}
Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1
TLDR
A crystal structure at 1.55 Å resolution revealed a highly unusual covalent product complex and biochemical studies investigated the function of a fully conserved active-site cysteine in glucosamine-6-phosphate N-acetyltransferase.
Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)
TLDR
It is anticipated that understanding of the structural basis behind the reaction and substrate specificity of the enzymes from this superfamily can be exploited in the development of novel therapeutics to treat human diseases and combat emerging multidrug-resistant microbial infections.
Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana.
TLDR
A phylogenetic analysis revealed that only one GNA isoform can be found in most of the species investigated and that the most likely Arabidopsis candidate is encoded by the gene At5g15770 (AtGNA), which has a very high structural similarity to crystallized GNA proteins from Homo sapiens and Saccharomyces cerevisiae despite less well conserved protein sequence identity.
The Mechanism of Acetyl Transfer Catalyzed by Mycobacterium tuberculosis GlmU
TLDR
The acetyltransferase substrate specificity and catalytic mechanism of the bifunctional N-acetyl transferase/uridylyltransferase from M. tuberculosis GlmU are reported, paving the way for the rational discovery of improved inhibitors against M.culosis.
Characterization, Localization, Essentiality, and High-Resolution Crystal Structure of Glucosamine 6-Phosphate N-Acetyltransferase from Trypanosoma brucei
TLDR
Analysis of the protein glycosylation phenotype of the TbGNA1 mutant under nonpermissive conditions revealed that poly-N-acetyllactosamine structures were greatly reduced in the parasite and that the glycosolation profile of the principal parasite surface coat component, the variant surface glycoprotein (VSG), was modified.
The Apicomplexa-specific glucosamine-6-phosphate N-acetyltransferase gene family encodes a key enzyme for glycoconjugate synthesis with potential as therapeutic target
TLDR
Sequence, phylogenetic and synteny analyses suggest an independent origin of the Apicomplexa-specific GNA1 family, parallel to the evolution of a different G NA1 family in other eukaryotes.
Human acetyl-CoA:glucosamine-6-phosphate N-acetyltransferase 1 has a relaxed donor specificity and transfers acyl groups up to four carbons in length.
TLDR
The goal of this work was to examine whether GNA1 has the ability to transfer a butyRYl group from butyryl-CoA to GlcN6P to form GlcNBu6P, which can then be converted to Gl cNBu.
GFPT2/GFAT2 and AMDHD2 act in tandem to control the hexosamine pathway
TLDR
A critical function of AMDHD2 is revealed in limiting UDP-GlcNAc production in cells that use GFPT2 for metabolite entry into the HBP, revealing a key role in metabolism, health, and aging.
Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases
TLDR
The results show that protein NATs have evolved more than once on the GNAT acetylation scaffold, indicating that N-terminal acetyltransferases do not constitute one homogeneous protein family, but that the ability to bind and acetylate protein N- termini had evolved more more thanOnce on the same acetylated scaffold.
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TLDR
Despite the diversity of substrate specificities, members of the GNAT superfamily demonstrate remarkable similarity in protein topology and mode of acetyl coenzyme A binding, likely reflecting a conserved catalytic mechanism.
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TLDR
Three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1 reveal a stable, β-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface and shed light on the catalytic machinery of GNA 1 at an atomic level, broadening the understanding of structural features required for GNAT activity.
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TLDR
This data indicates that suppression of N‐terminal acetyltransferases in Saccharomyces cerevisiae results in down-regulation of transcription regulation, histone deposition and histone displacement during spermatogenesis, although no known histone acetyl transferase is essential.
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