UDP-GlcNAc3NAcA | 112529-16-5

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: UDP-GlcNAc3NAcA
• 英文别名: UDP-alpha-D-GlcNAc3NAcA；(2S,3S,4R,5R,6R)-4,5-diacetamido-6-[[[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-3-hydroxyoxane-2-carboxylic acid
• CAS: 112529-16-5
• 化学式: C₁₉H₂₈N₄O₁₈P₂
• 分子量: 662.395
• InChiKey: GZLIMKLKXDFTJR-LTMKHLKMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.4
• 重原子数：
  43
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  326
• 氢给体数：
  9
• 氢受体数：
  18

反应信息

• 作为反应物：
  描述：

  UDP-GlcNAc3NAcA 在 WlbD 作用下， 生成 UDP-ManNAc3NAcA
  参考文献：
  名称：

  Molecular Structure of WlbB, a Bacterial N-Acetyltransferase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid,

  摘要：

  The pathogenic bacteria Pseudomonas aeruginosa and Bordetella pertussis contain in their outer membranes the rare sugar 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Five enzymes are required for the biosynthesis of this sugar starting from UDP-N-acetylglucosamine. One of these, referred to as WlbB, is an N-acetyltransferase that converts UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA) to UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NAcA). Here we report the three-dimensional structure of WlbB from Bordetella petrii. For this analysis, two ternary structures were determined to 1.43 angstrom resolution: one in which the protein was complexed with acetyl-CoA and UDP and the second in which the protein contained bound CoA and UDP-GlcNAc3NA. WlbB adopts a trimeric quaternary structure and belongs to the L beta H superfamily of N-acyltransferases. Each subunit contains 27 beta-strands, 23 of which form the canonical left-handed beta-helix. There are only two hydrogen bonds that occur between the protein and the GlcNAc3NA moiety, one between O-delta 1 of Asn 84 and the sugar C-3' amino group and the second between the backbone amide group of Arg 94 and the sugar C-5' carboxylate. The sugar C-3' amino group is ideally positioned in the active site to attack the si face of acetyl-CoA. Given that there are no protein side chains that can function as general bases within the GlcNAc3NA binding pocket, a reaction mechanism is proposed for WlbB whereby the sulfur of CoA ultimately functions as the proton acceptor required for catalysis.

  DOI：

  10.1021/bi1005738
• 作为产物：
  描述：

  尿苷5'-(2-乙酰氨基-2-脱氧-ALPHA-D-葡糖基焦磷酸酯) 在 硫酸氢铵 、 磷酸吡哆醛 、 β-烟酰胺腺嘌呤二核苷酸 、 monosodium glutamate 、 recombinant Psychrobacter cryohalolentis K₅^T N-acetyltransferase 、 recombinant Psychrobacter cryohalolentis K₅^T nicotinamide adenine dinucleotide (oxidized) (NAD+)-dependent dehydrogenase 、 recombinant Psychrobacter cryohalolentis K₅^T pyridoxal 5'-phosphate (PLP)-dependent aminotransferase 、 recombinant Psychrobacter cryohalolentis K₅^T uridine dinucleotide (UDP)-N-acetyl-D-glucosamine 6-dehydrogenase 作用下， 以 aq. buffer 为溶剂， 生成 UDP-GlcNAc3NAcA
  参考文献：
  名称：

  冷卤冷杆菌 K5T 生物合成 2,3-二乙酰氨基-2,3-二脱氧-d-葡萄糖醛酸所需酶的研究

  摘要：

  冷卤冷杆菌K5 T是一种革兰氏阴性细菌，于 2006 年首次从西伯利亚永久冻土中分离出来。它具有复杂的 O 抗原，含有L-鼠李糖、 D-半乳糖、两种二乙酰胺糖和一种三乙酰胺糖。其中一种二乙酰胺基糖，即2,3-二乙酰胺基-2,3-二脱氧-d-葡萄糖醛酸的生物合成途径目前尚不清楚。利用已发表的P.cryohalolentis K5 T基因组序列，我们假设Pcryo_0613 、 Pcryo_0614 、 Pcryo_0616和Pcryo_0615基因编码尿苷二核苷酸 (UDP) -N-乙酰基-d-葡萄糖胺 6-脱氢酶（一种烟酰胺腺嘌呤二核苷酸）分别是（氧化）（NAD + ）依赖性脱氢酶、5'-磷酸吡哆醛（PLP）依赖性氨基转移酶和N-乙酰转移酶，这些酶的活性是这种不寻常碳水化合物的生物合成所必需的。在这里，我们展示了这些假设蛋白质的克隆、过表达和纯化。 Pcryo_0613 、 Pcryo_0

  DOI：

  10.1002/pro.4502

文献信息

• Cofactor‐Driven Cascade Reactions Enable the Efficient Preparation of Sugar Nucleotides
  作者：Yuan Zheng、Jiabin Zhang、Jeffrey Meisner、Wanjin Li、Yawen Luo、Fangyu Wei、Liuqing Wen

  DOI：10.1002/anie.202115696

  日期：2022.5.9

  The complex de novo biosynthesis of sugar nucleotides was reorganized as cascade reactions. The cascade reactions were driven toward the formation of the target sugar nucleotides through the addition of an excess amount of a cofactor provided by a cofactor regeneration system, thus resulting in high synthetic yields.

  糖核苷酸的复杂从头生物合成被重组为级联反应。通过添加辅因子再生系统提供的过量辅因子，将级联反应驱动到目标糖核苷酸的形成，从而产生高合成产量。
• Molecular Structure of WlbB, a Bacterial <i>N</i>-Acetyltransferase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-<scp>d</scp>-mannuronic Acid,
  作者：James B. Thoden、Hazel M. Holden

  DOI：10.1021/bi1005738

  日期：2010.6.8

  The pathogenic bacteria Pseudomonas aeruginosa and Bordetella pertussis contain in their outer membranes the rare sugar 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Five enzymes are required for the biosynthesis of this sugar starting from UDP-N-acetylglucosamine. One of these, referred to as WlbB, is an N-acetyltransferase that converts UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA) to UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NAcA). Here we report the three-dimensional structure of WlbB from Bordetella petrii. For this analysis, two ternary structures were determined to 1.43 angstrom resolution: one in which the protein was complexed with acetyl-CoA and UDP and the second in which the protein contained bound CoA and UDP-GlcNAc3NA. WlbB adopts a trimeric quaternary structure and belongs to the L beta H superfamily of N-acyltransferases. Each subunit contains 27 beta-strands, 23 of which form the canonical left-handed beta-helix. There are only two hydrogen bonds that occur between the protein and the GlcNAc3NA moiety, one between O-delta 1 of Asn 84 and the sugar C-3' amino group and the second between the backbone amide group of Arg 94 and the sugar C-5' carboxylate. The sugar C-3' amino group is ideally positioned in the active site to attack the si face of acetyl-CoA. Given that there are no protein side chains that can function as general bases within the GlcNAc3NA binding pocket, a reaction mechanism is proposed for WlbB whereby the sulfur of CoA ultimately functions as the proton acceptor required for catalysis.
• Investigation of the enzymes required for the biosynthesis of 2, <scp>3‐</scp> diacetamido‐2,3‐dideoxy‐ <scp>d</scp> ‐glucuronic acid in <i>Psychrobacter cryohalolentis</i> <scp> K5 ^T </scp>
  作者：Daniel L. Hofmeister、Chase A. Seltzner、Nicholas J. Bockhaus、James B. Thoden、Hazel M. Holden

  DOI：10.1002/pro.4502

  日期：2023.1

  cryohalolentis K5T, we hypothesized that the genes designated Pcryo_0613, Pcryo_0614, Pcryo_0616, and Pcryo_0615 encode for a uridine dinucleotide (UDP)-N-acetyl-d-glucosamine 6-dehydrogenase, an nicotinamide adenine dinucleotide (oxidized) (NAD+)-dependent dehydrogenase, a pyridoxal 5′-phosphate (PLP)-dependent aminotransferase, and an N-acetyltransferase, respectively, activities of which would be required

  冷卤冷杆菌K5 T是一种革兰氏阴性细菌，于 2006 年首次从西伯利亚永久冻土中分离出来。它具有复杂的 O 抗原，含有L-鼠李糖、 D-半乳糖、两种二乙酰胺糖和一种三乙酰胺糖。其中一种二乙酰胺基糖，即2,3-二乙酰胺基-2,3-二脱氧-d-葡萄糖醛酸的生物合成途径目前尚不清楚。利用已发表的P.cryohalolentis K5 T基因组序列，我们假设Pcryo_0613 、 Pcryo_0614 、 Pcryo_0616和Pcryo_0615基因编码尿苷二核苷酸 (UDP) -N-乙酰基-d-葡萄糖胺 6-脱氢酶（一种烟酰胺腺嘌呤二核苷酸）分别是（氧化）（NAD + ）依赖性脱氢酶、5'-磷酸吡哆醛（PLP）依赖性氨基转移酶和N-乙酰转移酶，这些酶的活性是这种不寻常碳水化合物的生物合成所必需的。在这里，我们展示了这些假设蛋白质的克隆、过表达和纯化。 Pcryo_0613 、 Pcryo_0