80186-87-4Relevant academic research and scientific papers
D-Sedoheptulose-7-phosphate is a common precursor for the heptoses of septacidin and hygromycin B
Tang, Wei,Guo, Zhengyan,Cao, Zhenju,Wang, Min,Li, Pengwei,Meng, Xiangxi,Zhao, Xuejin,Xie, Zhoujie,Wang, Wenzhao,Zhou, Aihua,Lou, Chunbo,Chen, Yihua
, (2018)
Seven-carbon-chain–containing sugars exist in several groups of important bacterial natural products. Septacidin represents a group of L-heptopyranoses containing nucleoside antibiotics with antitumor, antifungal, and pain-relief activities. Hygromycin B,
COMPOSITIONS AND METHODS OF MODULATING THE IMMUNE RESPONSE BY ACTIVATING ALPHA PROTEIN KINASE 1
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Paragraph 470; 482; 483, (2019/05/15)
The disclosure provides compositions and methods related to activating alpha-kinase 1 (ALPK1) for modulating an immune response and treating or preventing cancer, infection, inflammation and related diseases and disorders as well as potentiating an immune response to a target antigen. The disclosure also provides heterocyclic compounds of formula (I) as agonists of alpha protein kinase 1 (ALPK1) and their use in activating ALPK1, modulating an immune response and treating diseases such as cancer, wherein A1, A2, L1, L2, L3, Z1, Z2, W1, W2, R1, R2, R3, R4, R5, R6 and R7 are defined herein.
Chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose and study of the substrate specificity of HldE
Li, Tiehai,Wen, Liuqing,Williams, Adriel,Wu, Baolin,Li, Lei,Qu, Jingyao,Meisner, Jeffrey,Xiao, Zhongying,Fang, Junqiang,Wang, Peng George
, p. 1139 - 1147 (2014/02/14)
An efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose (ADP-d, d-heptose) was reported using chemically synthesized d, d-heptose-7-phosphate and the ADP-d, d-heptose biosynthetic enzymes HldE and GmhB M
Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)
Wang, Liangbing,Huang, Hua,Nguyen, Henry H.,Allen, Karen N.,Mariano, Patrick S.,Dunaway-Mariano, Debra
experimental part, p. 1072 - 1081 (2010/11/21)
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-1α-GDP pathway (in S-layer glycoprotein biosynthesis) and the L-glycero-D-manno- heptose-1β-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-1β-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 1β,7-bisphosphate (kcat/K m=7 × 106 M-1 s-1) and D-glycero-D-manno-heptose 1α,7-bisphosphate (kcat/Km = 7 × 104 M-1 s-1) displayed physiologically significant substrate activity. 31P 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 1β-phosphate (Kis = 60 μM, and Kii = 150 μM) and histidinol phosphate (Kis = 1 mM, and Kii = 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 α- and β-anomers of D-glycero-D-manno-heptose 1β,7-bisphosphate catalyzed by the GmhB orthologs of the L-glycero-D-manno-heptose 1β-ADP pathways operative in Bordetella bronchiseptica and Mesorhizobium loti and by the GmhB of the D-glycero-D-manno-heptose 1α-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 β-anomer, whereas B. thetaiotaomicron GmhB is selective for the α-anomer. By determining the anomeric configuration of the physiological substrate (D-glycero-D-manno-heptose 1,7-bisphosphate) 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.
TOLL-LIKE RECEPTOR 9 AGONISTS
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Page/Page column 41, (2009/02/10)
The present invention provides TLR9 agonists comprising, as an active ingredient, a compound represented by formula (I): (wherein a represents 0 or 1; n represents an integer of 0 to 2; m represents an integer of 0 to 5; X1 and X2 each independently represent a hydrogen atom or hydroxy; Y represents an oxygen atom or a sulfur atom; -Q1-represents -O- or the like; -Q2- represents -O- or the like; -Z- represents -O- or the like; R1, R3 and R4 each independently represent hydroxy or the like; R2 and R5 each independently represent a hydrogen atom, hydroxy or the like; and A represents 6-aminopurin-9-yl or the like) or a pharmaceutically acceptable salt thereof, and the like.
Synthesis of DD-Heptose Phosphates as Substrates or Potential Inhibitors for the Heptose Synthetase
Paulsen, Hans,Pries, Meike,Lorentzen, Jens Peter
, p. 389 - 398 (2007/10/02)
A synthesis of D-glycero-D-manno-heptose (DD-Hep) via an inversion of L-glycero-D-manno-heptose (LD-Hep) is described.Starting from DD-Hep the α-1-phosphate 3 and the α-1-methylphosphonate 30 were synthesized.Furthermore, the α-1-dialkyldithiophosphate es
