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            <subfield code="a">10.1042/BCJ20180172</subfield>
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            <subfield code="2">sideral</subfield>
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            <subfield code="a">Raimi, O.G.</subfield>
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            <subfield code="a">Evidence for substrate-assisted catalysis in N-acetylphosphoglucosamine mutase</subfield>
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            <subfield code="c">2018</subfield>
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            <subfield code="a">N-acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wide range of glycans in eukaryotes. AGM belongs to the a-D-phosphohexomutase metalloenzyme superfamily and catalyzes the interconversion of N-acetylglucosamine-6-phosphate (GlcNAc-6P) to N-acetylglucosamine-1-phosphate (GlcNAc-1P) through N-acetylglucosa-mine-1, 6-bisphosphate (GlcNAc-1, 6-bisP) as the catalytic intermediate. Although there is an understanding of the phosphoserine-dependent catalytic mechanism at enzymatic and structural level, the identity of the requisite catalytic base in AGM1/phosphoglucomu-tases is as yet unknown. Here, we present crystal structures of a Michaelis complex of AGM1 with GlcNAc-6P and Mg2+, and a complex of the inactive Ser69Ala mutant together with glucose-1, 6-bisphosphate (Glc-1, 6-bisP) that represents key snapshots along the reaction co-ordinate. Together with mutagenesis, these structures reveal that the phosphate group of the hexose-1, 6-bisP intermediate may act as the catalytic base.</subfield>
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            <subfield code="a">BIOCHEMISTRY &amp; MOLECULAR BIOLOGY</subfield>
            <subfield code="b">72 / 294 = 0.245</subfield>
            <subfield code="c">2018</subfield>
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            <subfield code="a">Biochemistry</subfield>
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            <subfield code="a">Molecular Biology</subfield>
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            <subfield code="a">Cell Biology</subfield>
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            <subfield code="0">(orcid)0000-0002-3122-9401</subfield>
            <subfield code="a">Hurtado-Guerrero, R.</subfield>
            <subfield code="u">Universidad de Zaragoza</subfield>
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            <subfield code="a">Van Aalten, D.M.F.</subfield>
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            <subfield code="1">1002</subfield>
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            <subfield code="a">Universidad de Zaragoza</subfield>
            <subfield code="b">Dpto. Bioq.Biolog.Mol. Celular</subfield>
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            <subfield code="g">475, 15 (2018), 2547-2557</subfield>
            <subfield code="p">Biochem. j.</subfield>
            <subfield code="t">BIOCHEMICAL JOURNAL</subfield>
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            <subfield code="a">2020-01-17-22:06:19</subfield>
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