[(3R,4S,5S)-3,4,5-trihydroxy-2-oxohexyl] phosphate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: [(3R,4S,5S)-3,4,5-trihydroxy-2-oxohexyl] phosphate
• 化学式: C₆H₁₁O₈P
• 分子量: 242.122
• InChiKey: KNYGWWDTPGSEPD-FUTKDDECSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -3.5
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  150
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  [(3R,4S,5S)-3,4,5-trihydroxy-2-oxohexyl] phosphate 生成 (S)-乳醛 、 1,3-dihydroxyacetone phosphate
  参考文献：
  名称：

  L-鼠李糖-1-磷酸醛缩酶的结构和催化机理。

  摘要：

  L-鼠李糖-1-磷酸醛缩酶的结构已建立在1.35 A分辨率的晶体形式，这是通过表面突变获得的，并且在不对称单元中具有C（4）-对称四聚体的一个亚基。它证实了较早的2.7 A分辨率结构，该结构以复杂的晶体形式确定，每个不对称单元有20个亚基。链折叠和活性中心类似于L-岩藻糖-1-磷酸醛缩酶和L-核糖-5-磷酸4-表异构酶。所有三种酶的结构比较以及两种磷酸醛缩酶的产物磷酸二羟丙酮酯的抑制剂磷酸羟基羟异羟肟酸酯的结合模式都支持了活性中心的相似性。催化速率对几种突变的敏感性以及与相关醛缩酶的已建立机理的比较产生了推定的催化机理。该机理涉及两个醛缩酶中第二种产物L-丙醛的相同结合模式，除了醛基基团180度翻转以区分两个差向异构体鼠李糖和悬钩子。N末端结构域表现出相关的各向异性迁移率，该各向异性迁移率将各向同性布朗运动引导为N区域的催化碱和底物磷酸盐向C末端区域的锌离子和乳醛的定向运动。我们建议这种运

  DOI：

  10.1021/bi0349266
• 作为产物：
  描述：

  1,3-dihydroxyacetone phosphate 、 (S)-乳醛 在 L-rhamnulose-1-phosphate aldolase 作用下， 以 水 为溶剂， 反应 24.0h， 以100%的产率得到[(3R,4S,5S)-3,4,5-trihydroxy-2-oxohexyl] phosphate
  参考文献：
  名称：

  重新设计L-鼠李糖-1-磷酸醛缩酶对二羟基丙酮依赖性醛缩酶的磷酸结合位点

  摘要：

  据报道，由L-鼠李糖-1-磷酸醛缩酶（RhuA）（一种依赖于磷酸二羟基丙酮的醛缩酶）催化的醛基中的未磷酸化二羟基丙酮（DHA）醛缩醛加成反应。此外，RhuA野生型磷酸结合位点的单点突变，即在N29位用天冬氨酸取代天冬酰胺，使DHA与其他醛受体而不是天然L的羟醛加成反应增加了3倍。丙醛 RhuA N29D突变体修改了天然底物的最佳酶设计，并改变了其催化性能，使醛缩酶比其他添加DHA的醛缩酶更具通用性。

  DOI：

  10.1002/adsc.201000719

文献信息

• Antenna Domain Mobility and Enzymatic Reaction of <scp>l</scp>-Rhamnulose-1-phosphate Aldolase^,
  作者：Dirk Grueninger、Georg E. Schulz

  DOI：10.1021/bi7012799

  日期：2008.1.1

  The enzyme l-rhamnulose-1-phosphate aldolase from Escherichia coli participates in the degradation pathway of l-rhamnose, a ubiquitous deoxy-hexose. It is a homotetramer of the rare C4-symmetric type with N-terminal domains protruding like antennas from the main body. A mobility analysis of the enzyme gave rise to the hypothesis that an anisotropic thermal antenna motion may support the catalysis (Kroemer et al., Biochemistry 42, 10560, 2003). We checked this hypothesis by generating four single mutants and one disulfide bridge that were designed to reduce the mobility of the antenna domain without disturbing the chain-fold or the active center. The catalytic rates of the mutants revealed activity reductions that correlated well with the expected antenna fixation. Among these mutants, K15W was crystallized, structurally elucidated, and used as a guide for modeling the others. The structure confirmed the design because the mutation introduced a tight nonpolar contact to a neighboring subunit that fixed the antenna but did not affect the main chain. The fixation was confirmed by a comparison of the anisotropic B-factors describing the mobility of the domains. It turned out that the distinctly anisotropic mobility of the wild-type antenna domain has become isotropic in K15W, in agreement with the design. We suggest that, like K15W, the other mutations also followed the design, validating the correlation between antenna mobility and activity. This correlation suggests that the domain mobility facilitates the reaction.
• METABOLISM OF <scp>l</scp> -RHAMNOSE BY <i>ESCHERICHIA COLI</i>
  作者：Dorothy M. Wilson、Sam Ajl

  DOI：10.1128/jb.73.3.415-420.1957

  日期：1957.3
• The purification and properties of l-rhamnulokinase
  作者：T.H. Chiu、David Sidney Feingold

  DOI：10.1016/0926-6569(64)90009-4

  日期：1964.12
• Structure and Reaction Mechanism of l-Rhamnulose Kinase from Escherichia coli
  作者：Dirk Grueninger、Georg E. Schulz

  DOI：10.1016/j.jmb.2006.04.013

  日期：2006.6

  Bacterial L-rhamnulose kinase participates in the degradation of L-rhamnose, which is ubiquitous and particularly abundant in some plants. The enzyme catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose. We determined the crystal structures of the substrate-free kinase and of a complex between the enzyme, ADP and L-fructose, which besides rhamnulose is also processed. According to its chainfold, the kinase belongs to the hexokinase-hsp70-actin superfamily. The closest structurally known homologue is glycerol kinase. The reported structures reveal a large conformational change on substrate binding as well as the key residues involved in catalysis. The substrates ADP and P-L-fructose are in an ideal position to define a direct in-line phosphoryl transfer through a bipyramidal pentavalent intermediate. The enzyme contains one disulfide bridge at a position where two homologous glycerol kinases are regulated by phosphorylation and effector binding, respectively, and it has two more pairs of cysteine residues near the surface that are poised for bridging. However, identical catalytic rates were observed for the enzyme in reducing and oxidizing environments, suggesting that regulation by disulfide formation is unlikely. (c) 2006 Elsevier Ltd. All rights reserved.