Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline D-galactosamine 6-phosphate Identifier CHEBI:71674 Charge -1 Formula C6H13NO8P InChIKeyhelp_outline XHMJOUIAFHJHBW-GASJEMHNSA-M SMILEShelp_outline [NH3+][C@H]1C(O)O[C@H](COP([O-])([O-])=O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-galactosamine 1-phosphate Identifier CHEBI:142399 Charge -1 Formula C6H13NO8P InChIKeyhelp_outline YMJBYRVFGYXULK-VFUOTHLCSA-M SMILEShelp_outline [C@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O)[NH3+])OP([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:46048 | RHEA:46049 | RHEA:46050 | RHEA:46051 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii.
Dadashipour M., Iwamoto M., Hossain M.M., Akutsu J.I., Zhang Z., Kawarabayasi Y.
Most organisms, from <i>Bacteria</i> to <i>Eukarya</i>, synthesize UDP-<i>N</i>-acetylglucosamine (UDP-GlcNAc) from fructose-6-phosphate via a four-step reaction, and UDP-<i>N</i>-acetylgalactosamine (UDP-GalNAc) can only be synthesized from UDP-GlcNAc by UDP-GlcNAc 4-epimerase. In <i>Archaea</i>, ... >> More
Most organisms, from <i>Bacteria</i> to <i>Eukarya</i>, synthesize UDP-<i>N</i>-acetylglucosamine (UDP-GlcNAc) from fructose-6-phosphate via a four-step reaction, and UDP-<i>N</i>-acetylgalactosamine (UDP-GalNAc) can only be synthesized from UDP-GlcNAc by UDP-GlcNAc 4-epimerase. In <i>Archaea</i>, the bacterial-type UDP-GlcNAc biosynthetic pathway was reported for <i>Methanococcales.</i> However, the complete biosynthetic pathways for UDP-GlcNAc and UDP-GalNAc present in one archaeal species are unidentified. Previous experimental analyses on enzymatic activities of the ST0452 protein, identified from the thermophilic crenarchaeon <i>Sulfolobus tokodaii</i>, predicted the presence of both a bacterial-type UDP-GlcNAc and an independent UDP-GalNAc biosynthetic pathway in this archaeon. In the present work, functional analyses revealed that the recombinant ST2186 protein possessed an glutamine:fructose-6-phosphate amidotransferase activity and that the recombinant ST0242 protein possessed a phosphoglucosamine-mutase activity. Along with the acetyltransferase and uridyltransferase activities of the ST0452 protein, the activities of the ST2186 and ST0242 proteins confirmed the presence of a bacterial-type UDP-GlcNAc biosynthetic pathway in <i>S. tokodaii</i> In contrast, the UDP-GlcNAc 4-epimerase homologue gene was not detected within the genomic data. Thus, it was expected that galactosamine-1-phosphate or galactosamine-6-phosphate (GalN-6-P) was provided by conversion of glucosamine-1-phosphate or glucosamine-6-phosphate (GlcN-6-P). A novel epimerase converting GlcN-6-P to GalN-6-P was detected in a cell extract of <i>S. tokodaii</i>, and the N-terminal sequence of the purified protein indicated that the novel epimerase was encoded by the ST2245 gene. Along with the ST0242 phosphogalactosamine-mutase activity, this observation confirmed the presence of a novel UDP-GalNAc biosynthetic pathway from GlcN-6-P in <i>S. tokodaii</i> Discovery of the novel pathway provides a new insight into the evolution of nucleotide sugar metabolic pathways.<b>IMPORTANCE</b> In this work, a novel protein capable of directly converting glucosamine-6-phosphate to galactosamine-6-phosphate was successfully purified from a cell extract of the thermophilic crenarchaeon <i>Sulfolobus tokodaii</i> Confirmation of this novel activity using the recombinant protein indicates that <i>S. tokodaii</i> possesses a novel UDP-GalNAc biosynthetic pathway derived from glucosamine-6-phosphate. The distributions of this and related genes indicate the presence of three different types of UDP-GalNAc biosynthetic pathways: a direct pathway using a novel enzyme and two conversion pathways from UDP-GlcNAc using known enzymes. Additionally, <i>Crenarchaeota</i> species lacking all three pathways were found, predicting the presence of one more unknown pathway. Identification of these novel proteins and pathways provides important insights into the evolution of nucleotide sugar biosynthesis, as well as being potentially important industrially. << Less
J. Bacteriol. 200:E00048-E00048(2018) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.