甘露糖-1,6-二磷酸酯 | 19504-70-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 甘露糖-1,6-二磷酸酯
• 英文名称: D-mannose 1α,6-bisphosphate
• 英文别名: D-mannopyranose 1α,6-bisphosphate；O¹,O⁶-Diphosphono-α-D-mannopyranose；Mannose-1,6-bisphosphate；[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(phosphonooxymethyl)oxan-2-yl] dihydrogen phosphate
• CAS: 19504-70-2
• 化学式: C₆H₁₄O₁₂P₂
• 分子量: 340.117
• InChiKey: RWHOZGRAXYWRNX-RWOPYEJCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.3
• 重原子数：
  20
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  203
• 氢给体数：
  7
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  D-mannopyranose 6-phosphate 在 recombinant A. thermoaerophilus [α-C(1)OH specific] D-glycero-D-manno-heptose-7-P kinase 、 adenosine 5'-triphosphate disodium salt 、 magnesium chloride 作用下， 反应 36.0h， 以470 mg的产率得到甘露糖-1,6-二磷酸酯
  参考文献：
  名称：

  Divergence of Biochemical Function in the HAD Superfamily: d-glycero-d-manno-Heptose-1,7-bisphosphate Phosphatase (GmhB)

  摘要：

  D-glycero-D-manno-Heptose-1,7-bisphosphate phosphatase (GmhB) is a member of the histidinol-phosphate phosphatase (HisB) subfamily of the haloalkanoic acid dehalogenase (HAD) enzyme superfamily. GmhB supports two divergent biochemical pathways in bacteria: the D-glycero-D-manno-heptose-1 alpha-GDP pathway (in S-layer glycoprotein biosynthesis) and the L-glycero-D-manno-heptose-1 beta-ADP pathway (in lipid A biosynthesis). Herein, we report the comparative analysis Of Substrate recognition in selected GmhB orthologs. The substrate specificity of the L-glycero-D-manno-heptose-1 beta-ADP pathway GmhB from Escherichia coli K-12 was evaluated using hexose and heptose bisphosphates, histidinol phosphate, and common organophosphate metabolites. Only D-glycero-D-manno-heptose 1 beta,7-bisphosphate (k(cat)/k(m) = 7 x 10(6) M-1 s(-1)) and D-glycero-D-manno-heptose 1 alpha,7-bisphosphate (k(cat)/K-m, = 7 x 10(4) M-1 s(-1)) displayed physiologically significant Substrate activity. P-31 NMR analysis demonstrated that E. coli GmhB selectively removes the C(7) phosphate. Steady-state kinetic inhibition studies showed that D-glycero-D-manno-heptose 1 beta-phosphate (K-is = 60 mu M, and K-ii = 150 mu M) and histidinol phosphate (K-is = 1 mM, and K-ii = 6 mM), while not hydrolyzed, do in fact bind to E. coli GmhB, which leads to the conclusion that nonproductive binding contributes to substrate discrimination. High catalytic efficiency and a narrow substrate range are characteristic of a well-evolved metabolic enzyme, and as such, E. coli GmhB is set apart from most HAD phosphatases (which are typically inefficient and promiscuous). The specialization of the biochemical function of GmhB was examined by measuring the kinetic constants for hydrolysis of the alpha- and beta-anomers of D-glycero-D-manno-heptose 1 beta,7-bisphosphate catalyzed by the GmhB orthologs of the L-glycero-D-manno- 1 beta-ADP pathways operative in Bordetella bronchiseptica and Mesorhizobium and by the GmhB of the D-glycero-D-manno-heptose 1 alpha-GDP pathway operative in Bacteroides thetaiotaomicron. The results show that although each of these representatives possesses physiologically significant catalytic activity toward both anomers, each displays substantial anomeric specificity. Like E. coli GmhB, B. bronchiseptica GmhB and M. loti GmhB prefer the beta-anomer, whereas B. thetaiotaomicron GmhB is selective for the alpha-anomer. By determining the anomeric configuration of the physiological Substrate (D-glycero-D-manno-heptose 1,7- for each of the four GmhB orthologs, we discovered that the anomeric specificity of GmhB correlates with that of the pathway kinase. The conclusion drawn from this finding is that the evolution of the ancestor to GmhB in the HisB subfamily provided for specialization toward two distinct biochemical functions.

  DOI：

  10.1021/bi902018y

文献信息

• Synth�ses d'esters phosphoriques d'int�r�t biologique III. Synth�se des acides ?-D-mannose-1-phosphorique, D-mannose-6-phosphorique et ?-D-mannose-1,6-diphosphorique. Action de la phosphoglucomutase
  作者：Th. Posternak、J. P. Rosselet

  DOI：10.1002/hlca.19530360649

  日期：——

  L'acide α-D-mannose-1-phosphorique a été préparé par condensation de l'acétochloromannose avec le diphénylphosphate d'argent, suivie d'hydrogénolyse et de désacétylation. Par la même méthode on a obtenu l'acide α-D-mannose-1,6-diphosphorique à partir du chlorure de triacétyl-2,3,4-diphénylphosphoryl-6-mannosyle α.

  酰胺化的α-D-甘露糖-1-磷酸，乙酰化的氯甘露糖，二羟基磷酸酯化的二苯醚，氢化的糖基化酶等。用酰胺化的α-D-甘露糖-1,6-二磷酸在三氯叔丁基-2,3,4-二苯甲基磷酰基-6-甘露糖基α上的同化酶处理。
• Divergence of Biochemical Function in the HAD Superfamily: <scp>d</scp>-<i>glycero</i>-<scp>d</scp><i>-manno-</i>Heptose-1,7-bisphosphate Phosphatase (GmhB)
  作者：Liangbing Wang、Hua Huang、Henry H. Nguyen、Karen N. Allen、Patrick S. Mariano、Debra Dunaway-Mariano

  DOI：10.1021/bi902018y

  日期：2010.2.16

  D-glycero-D-manno-Heptose-1,7-bisphosphate phosphatase (GmhB) is a member of the histidinol-phosphate phosphatase (HisB) subfamily of the haloalkanoic acid dehalogenase (HAD) enzyme superfamily. GmhB supports two divergent biochemical pathways in bacteria: the D-glycero-D-manno-heptose-1 alpha-GDP pathway (in S-layer glycoprotein biosynthesis) and the L-glycero-D-manno-heptose-1 beta-ADP pathway (in lipid A biosynthesis). Herein, we report the comparative analysis Of Substrate recognition in selected GmhB orthologs. The substrate specificity of the L-glycero-D-manno-heptose-1 beta-ADP pathway GmhB from Escherichia coli K-12 was evaluated using hexose and heptose bisphosphates, histidinol phosphate, and common organophosphate metabolites. Only D-glycero-D-manno-heptose 1 beta,7-bisphosphate (k(cat)/k(m) = 7 x 10(6) M-1 s(-1)) and D-glycero-D-manno-heptose 1 alpha,7-bisphosphate (k(cat)/K-m, = 7 x 10(4) M-1 s(-1)) displayed physiologically significant Substrate activity. P-31 NMR analysis demonstrated that E. coli GmhB selectively removes the C(7) phosphate. Steady-state kinetic inhibition studies showed that D-glycero-D-manno-heptose 1 beta-phosphate (K-is = 60 mu M, and K-ii = 150 mu M) and histidinol phosphate (K-is = 1 mM, and K-ii = 6 mM), while not hydrolyzed, do in fact bind to E. coli GmhB, which leads to the conclusion that nonproductive binding contributes to substrate discrimination. High catalytic efficiency and a narrow substrate range are characteristic of a well-evolved metabolic enzyme, and as such, E. coli GmhB is set apart from most HAD phosphatases (which are typically inefficient and promiscuous). The specialization of the biochemical function of GmhB was examined by measuring the kinetic constants for hydrolysis of the alpha- and beta-anomers of D-glycero-D-manno-heptose 1 beta,7-bisphosphate catalyzed by the GmhB orthologs of the L-glycero-D-manno- 1 beta-ADP pathways operative in Bordetella bronchiseptica and Mesorhizobium and by the GmhB of the D-glycero-D-manno-heptose 1 alpha-GDP pathway operative in Bacteroides thetaiotaomicron. The results show that although each of these representatives possesses physiologically significant catalytic activity toward both anomers, each displays substantial anomeric specificity. Like E. coli GmhB, B. bronchiseptica GmhB and M. loti GmhB prefer the beta-anomer, whereas B. thetaiotaomicron GmhB is selective for the alpha-anomer. By determining the anomeric configuration of the physiological Substrate (D-glycero-D-manno-heptose 1,7- for each of the four GmhB orthologs, we discovered that the anomeric specificity of GmhB correlates with that of the pathway kinase. The conclusion drawn from this finding is that the evolution of the ancestor to GmhB in the HisB subfamily provided for specialization toward two distinct biochemical functions.