Wang AH

References (10)

Title : Euphorfinoids E-L: Diterpenoids from the roots of Euphorbia fischeriana with acetylcholinesterase inhibitory activity - Wei_2021_Phytochemistry_190_112867
Author(s) : Wei JC , Zhang XY , Gao YN , Wang DD , He XL , Gao XX , Hu GS , Wang AH , Jia JM
Ref : Phytochemistry , 190 :112867 , 2021
Abstract : Eight undescribed diterpenoids, euphorfinoids E-L, together with twelve known analogues, were isolated from the roots of wild Euphorbia fischeriana. Their structures and absolute configurations were elucidated by a combination of NMR, MS, ECD, and X-ray diffraction analyses. The plausible biosynthetic pathway of 1 was also proposed. The isolated compounds displayed moderate inhibitory activity against acetylcholinesterase (AChE) with 50% inhibiting concentration (IC(50)) values of 6.23-192.38 microM.
ESTHER : Wei_2021_Phytochemistry_190_112867
PubMedSearch : Wei_2021_Phytochemistry_190_112867
PubMedID: 34304117

Title : Diterpenoids from the roots of Euphorbia ebracteolata and their inhibitory effects on human carboxylesterase 2 - Wang_2017_Phytochemistry_146_82
Author(s) : Wang AH , Tian XG , Cui YL , Huo XK , Zhang BJ , Deng S , Feng L , Ma XC , Jia JM , Wang C
Ref : Phytochemistry , 146 :82 , 2017
Abstract : A chemical investigation of the roots of Euphorbia ebracteolata identified eighteen diterpenoids and glycosides. On the basis of spectroscopic data, they were determined to be ent-kauranes, ent-atisanes, tigliane derivatives, ingenane, and ent-abietanes, among which were eleven previously undescribed diterpenoids. The inhibitory effects of the isolated compounds against human carboxylesterase 2 (hCE-2) were evaluated in vitro, which revealed moderate inhibitory effects with IC50 values<50muM. Next, the inhibitory kinetics were evaluated for the putative hCE-2 inhibitor 4beta,9alpha,16,20-tetrahydroxy-14(13-->12)-abeo-12alphaH-1,6-tigliadiene-3,13-di one (IC50 3.88muM), and results indicated competitive inhibition with Ki 4.94muM. Additionally, none of the diterpenoids showed cytotoxic effects against five human tumor cell lines as determined by MTT assays.
ESTHER : Wang_2017_Phytochemistry_146_82
PubMedSearch : Wang_2017_Phytochemistry_146_82
PubMedID: 29253734

Title : Chemical characteristics of the fungus Ganoderma lucidum and their inhibitory effects on acetylcholinesterase - Wei_2017_J.Asian.Nat.Prod.Res__1
Author(s) : Wei JC , Wang AH , Wei YL , Huo XK , Tian XG , Feng L , Ma XC , Wang C , Huang SS , Jia JM
Ref : J Asian Nat Prod Res , :1 , 2017
Abstract : The chemical characteristic of a well-known folk medicine Ganoderma lucidum has been investigated by a series of chromatographic technologies, which displayed the presences of 45 lanostane type triterpenoids, including two new nor-lanostane triterpenoids (40, 41). Their structures were identified on the basis of spectroscopic data analysis (UV, IR, HRESIMS, 1D, and 2D NMR). Notably, some triterpenoids displayed moderate inhibitory effects against AChE (acetylcholinesterase) by an in vitro screened experiment. Triterpenoid 2 displayed the potent inhibitory effect with IC50 10.8 and Ki 14.95 muM (inhibition kinetic). The preliminary SAR has been discussed by the docking analyses between ganoderic acids (1, 2) and AChE.
ESTHER : Wei_2017_J.Asian.Nat.Prod.Res__1
PubMedSearch : Wei_2017_J.Asian.Nat.Prod.Res__1
PubMedID: 28944681

Title : Phenolic glycosides and monoterpenoids from the roots of Euphorbia ebracteolata and their bioactivities - Wang_2017_Fitoterapia_121_175
Author(s) : Wang AH , Huo XK , Feng L , Sun CP , Deng S , Zhang HL , Zhang BJ , Ma XC , Jia JM , Wang C
Ref : Fitoterapia , 121 :175 , 2017
Abstract : The bioactive substance investigation of Euphorbia ebracteolata obtained 17 compounds by various chromatographic techniques. Their structures were elucidated using widely spectroscopic data, including ESI-MS, HRESI-MS, CD, 1D- and 2D-NMR, which gave 5 new phenolic glucosides and 4 new monoterpenoids. The phenolic glucosides and monoterpenoids showed the inhibitory effect against the human carboxylesterase-2 (hCE-2) using a fluorescence bioassay in vitro, with the strongest inhibitor compound 4 (IC50 7.17muM). The antioxidant effects of these isolated compounds were evaluated using a DPPH scavenging assay. All of the phenolic acids displayed the DPPH scavenging effect, especially that eight compounds have better effect than vitamin C, with the IC50 values ranging from 4.52 to 7.52muM. Additionally, compounds 1-17 showed no cytotoxic effect against five human cancer cell lines by MTT assay.
ESTHER : Wang_2017_Fitoterapia_121_175
PubMedSearch : Wang_2017_Fitoterapia_121_175
PubMedID: 28760607

Title : Crystal structure of vespid phospholipase A1 reveals insights into the mechanism for cause of membrane dysfunction - Hou_2016_Insect.Biochem.Mol.Biol_68_79
Author(s) : Hou MH , Chuang CY , Ko TP , Hu NJ , Chou CC , Shih YP , Ho CL , Wang AH
Ref : Insect Biochemistry & Molecular Biology , 68 :79 , 2016
Abstract : Vespid phospholipase A1 (vPLA1) from the black-bellied hornet (Vespa basalis) catalyzes the hydrolysis of emulsified phospholipids and shows potent hemolytic activity that is responsible for its lethal effect. To investigate the mechanism of vPLA1 towards its function such as hemolysis and emulsification, we isolated vPLA1 from V. basalis venom and determined its crystal structure at 2.5 A resolution. vPLA1 belongs to the alpha/beta hydrolase fold family. It contains a tightly packed beta-sheet surrounded by ten alpha-helices and a Gly-X-Ser-X-Gly motif, characteristic of a serine hydrolyase active site. A bound phospholipid was modeled into the active site adjacent to the catalytic Ser-His-Asp triad indicating that Gln95 is located at hydrogen-bonding distance from the substrate's phosphate group. Moreover, a hydrophobic surface comprised by the side chains of Phe53, Phe62, Met91, Tyr99, Leu197, Ala167 and Pro169 may serve as the acyl chain-binding site. vPLA1 shows global similarity to the N-terminal domain of human pancreatic lipase (HPL), but with some local differences. The lid domain and the beta9 loop responsible for substrate selectivity in vPLA1 are shorter than in HPL. Thus, solvent-exposed hydrophilic residues can easily accommodate the polar head groups of phospholipids, thereby accounting for the high activity level of vPLA1. Our result provides a potential explanation for the ability of vPLA1 to hydrolyze phospholipids of cell membrane.
ESTHER : Hou_2016_Insect.Biochem.Mol.Biol_68_79
PubMedSearch : Hou_2016_Insect.Biochem.Mol.Biol_68_79
PubMedID: 26603193
Gene_locus related to this paper: vesba-pa1

Title : Structural insights into enzymatic degradation of oxidized polyvinyl alcohol - Yang_2014_Chembiochem_15_1882
Author(s) : Yang Y , Ko TP , Liu L , Li J , Huang CH , Chan HC , Ren F , Jia D , Wang AH , Guo RT , Chen J , Du G
Ref : Chembiochem , 15 :1882 , 2014
Abstract : The ever-increasing production and use of polyvinyl alcohol (PVA) threaten our environment. Yet PVA can be assimilated by microbes in two steps: oxidation and cleavage. Here we report novel alpha/beta-hydrolase structures of oxidized PVA hydrolase (OPH) from two known PVA-degrading organisms, Sphingopyxis sp. 113P3 and Pseudomonas sp. VM15C, including complexes with substrate analogues, acetylacetone and caprylate. The active site is covered by a lid-like beta-ribbon. Unlike other esterase and amidase, OPH is unique in cleaving the CC bond of beta-diketone, although it has a catalytic triad similar to that of most alpha/beta-hydrolases. Analysis of the crystal structures suggests a double-oxyanion-hole mechanism, previously only found in thiolase cleaving beta-ketoacyl-CoA. Three mutations in the lid region showed enhanced activity, with potential in industrial applications.
ESTHER : Yang_2014_Chembiochem_15_1882
PubMedSearch : Yang_2014_Chembiochem_15_1882
PubMedID: 25044912
Gene_locus related to this paper: psesp-OPH , sphs1-OPH

Title : The dimeric transmembrane domain of prolyl dipeptidase DPP-IV contributes to its quaternary structure and enzymatic activities - Chung_2010_Protein.Sci_19_1627
Author(s) : Chung KM , Cheng JH , Suen CS , Huang CH , Tsai CH , Huang LH , Chen YR , Wang AH , Jiaang WT , Hwang MJ , Chen X
Ref : Protein Science , 19 :1627 , 2010
Abstract : Dipeptidyl peptidase IV (DPP-IV) is a drug target in the treatment of human type II diabetes. It is a type II membrane protein with a single transmembrane domain (TMD) anchoring the extracellular catalytic domain to the membrane. DPP-IV is active as a dimer, with two dimer interacting surfaces located extracellularly. In this study, we demonstrate that the TM of DPP-IV promotes DPP-IV dimerization and rescues monomeric DPP-IV mutants into partial dimers, which is specific and irreplaceable by TMs of other type II membrane proteins. By bioluminescence resonance energy transfer (BRET) and peptide electrophoresis, we found that the TM domain of DPP-IV is dimerized in mammalian cells and in vitro. The TM dimer interaction is very stable, based on our results with TM site-directed mutagenesis. None of the mutations, including the introduction of two prolines, resulted in their complete disruption to monomers. However, these TM proline mutations result in a significant reduction of DPP-IV enzymatic activity, comparable to what is found with mutations near the active site. A systematic analysis of TM structures deposited in the Protein Data Bank showed that prolines in the TM generally produce much bigger kinking angles than occur in nonproline-containing TMs. Thus, the proline-dependent reduction in enzyme activity may result from propagated conformational changes from the TM to the extracellular active site. Our results demonstrate that TM dimerization and conformation contribute significantly to the structure and activity of DPP-IV. Optimal enzymatic activity of DPP-IV requires an optimal interaction of all three dimer interfaces, including its TM.
ESTHER : Chung_2010_Protein.Sci_19_1627
PubMedSearch : Chung_2010_Protein.Sci_19_1627
PubMedID: 20572019

Title : Structure of the alkalohyperthermophilic Archaeoglobus fulgidus lipase contains a unique C-terminal domain essential for long-chain substrate binding - Chen_2009_J.Mol.Biol_390_672
Author(s) : Chen CK , Lee GC , Ko TP , Guo RT , Huang LM , Liu HJ , Ho YF , Shaw JF , Wang AH
Ref : Journal of Molecular Biology , 390 :672 , 2009
Abstract : Several crystal structures of AFL, a novel lipase from the archaeon Archaeoglobus fulgidus, complexed with various ligands, have been determined at about 1.8 A resolution. This enzyme has optimal activity in the temperature range of 70-90 degrees C and pH 10-11. AFL consists of an N-terminal alpha/beta-hydrolase fold domain, a small lid domain, and a C-terminal beta-barrel domain. The N-terminal catalytic domain consists of a 6-stranded beta-sheet flanked by seven alpha-helices, four on one side and three on the other side. The C-terminal lipid binding domain consists of a beta-sheet of 14 strands and a substrate covering motif on top of the highly hydrophobic substrate binding site. The catalytic triad residues (Ser136, Asp163, and His210) and the residues forming the oxyanion hole (Leu31 and Met137) are in positions similar to those of other lipases. Long-chain lipid is located across the two domains in the AFL-substrate complex. Structural comparison of the catalytic domain of AFL with a homologous lipase from Bacillus subtilis reveals an opposite substrate binding orientation in the two enzymes. AFL has a higher preference toward long-chain substrates whose binding site is provided by a hydrophobic tunnel in the C-terminal domain. The unusually large interacting surface area between the two domains may contribute to thermostability of the enzyme. Two amino acids, Asp61 and Lys101, are identified as hinge residues regulating movement of the lid domain. The hydrogen-bonding pattern associated with these two residues is pH dependent, which may account for the optimal enzyme activity at high pH. Further engineering of this novel lipase with high temperature and alkaline stability will find its use in industrial applications.
ESTHER : Chen_2009_J.Mol.Biol_390_672
PubMedSearch : Chen_2009_J.Mol.Biol_390_672
PubMedID: 19447113
Gene_locus related to this paper: arcfu-AF1763

Title : Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha\/beta-hydrolase - Yang_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_498
Author(s) : Yang CY , Chin KH , Chou CC , Wang AH , Chou SH
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 62 :498 , 2006
Abstract : XC6422 is a conserved hypothetical protein from Xanthomonas campestris pathovar campestris (Xcc), a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. The protein consists of 220 amino acids and its structure has been determined to 1.6 A resolution using the multi-wavelength anomalous dispersion (MAD) method. Although it has very low sequence identity to protein sequences in the PDB (less than 20%), the determined structure nevertheless shows that it belongs to the superfamily of serine alpha/beta-hydrolases, with an active site that is fully accessible to solvent owing to the absence of a lid domain. Modelling studies with the serine esterase inhibitor E600 indicate that XC6422 adopts a conserved Ser-His-Asp catalytic triad common to this superfamily and has a preformed oxyanion hole for catalytic activation. These structural features suggest that XC6422 is most likely to be a hydrolase active on a soluble ester or a small lipid. An extra strand preceding the first beta-strand in the canonical alpha/beta-hydrolase fold leads to extensive subunit interactions between XC6422 monomers, which may explain why XC6422 crystals of good diffraction quality can grow to dimensions of up to 1.5 mm in a few days.
ESTHER : Yang_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_498
PubMedSearch : Yang_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_498
PubMedID: 16754966
Gene_locus related to this paper: xanca-XC6422

Title : The genome sequence of Drosophila melanogaster - Adams_2000_Science_287_2185
Author(s) : Adams MD , Celniker SE , Holt RA , Evans CA , Gocayne JD , Amanatides PG , Scherer SE , Li PW , Hoskins RA , Galle RF , George RA , Lewis SE , Richards S , Ashburner M , Henderson SN , Sutton GG , Wortman JR , Yandell MD , Zhang Q , Chen LX , Brandon RC , Rogers YH , Blazej RG , Champe M , Pfeiffer BD , Wan KH , Doyle C , Baxter EG , Helt G , Nelson CR , Gabor GL , Abril JF , Agbayani A , An HJ , Andrews-Pfannkoch C , Baldwin D , Ballew RM , Basu A , Baxendale J , Bayraktaroglu L , Beasley EM , Beeson KY , Benos PV , Berman BP , Bhandari D , Bolshakov S , Borkova D , Botchan MR , Bouck J , Brokstein P , Brottier P , Burtis KC , Busam DA , Butler H , Cadieu E , Center A , Chandra I , Cherry JM , Cawley S , Dahlke C , Davenport LB , Davies P , de Pablos B , Delcher A , Deng Z , Mays AD , Dew I , Dietz SM , Dodson K , Doup LE , Downes M , Dugan-Rocha S , Dunkov BC , Dunn P , Durbin KJ , Evangelista CC , Ferraz C , Ferriera S , Fleischmann W , Fosler C , Gabrielian AE , Garg NS , Gelbart WM , Glasser K , Glodek A , Gong F , Gorrell JH , Gu Z , Guan P , Harris M , Harris NL , Harvey D , Heiman TJ , Hernandez JR , Houck J , Hostin D , Houston KA , Howland TJ , Wei MH , Ibegwam C , Jalali M , Kalush F , Karpen GH , Ke Z , Kennison JA , Ketchum KA , Kimmel BE , Kodira CD , Kraft C , Kravitz S , Kulp D , Lai Z , Lasko P , Lei Y , Levitsky AA , Li J , Li Z , Liang Y , Lin X , Liu X , Mattei B , McIntosh TC , McLeod MP , McPherson D , Merkulov G , Milshina NV , Mobarry C , Morris J , Moshrefi A , Mount SM , Moy M , Murphy B , Murphy L , Muzny DM , Nelson DL , Nelson DR , Nelson KA , Nixon K , Nusskern DR , Pacleb JM , Palazzolo M , Pittman GS , Pan S , Pollard J , Puri V , Reese MG , Reinert K , Remington K , Saunders RD , Scheeler F , Shen H , Shue BC , Siden-Kiamos I , Simpson M , Skupski MP , Smith T , Spier E , Spradling AC , Stapleton M , Strong R , Sun E , Svirskas R , Tector C , Turner R , Venter E , Wang AH , Wang X , Wang ZY , Wassarman DA , Weinstock GM , Weissenbach J , Williams SM , WoodageT , Worley KC , Wu D , Yang S , Yao QA , Ye J , Yeh RF , Zaveri JS , Zhan M , Zhang G , Zhao Q , Zheng L , Zheng XH , Zhong FN , Zhong W , Zhou X , Zhu S , Zhu X , Smith HO , Gibbs RA , Myers EW , Rubin GM , Venter JC
Ref : Science , 287 :2185 , 2000
Abstract : The fly Drosophila melanogaster is one of the most intensively studied organisms in biology and serves as a model system for the investigation of many developmental and cellular processes common to higher eukaryotes, including humans. We have determined the nucleotide sequence of nearly all of the approximately 120-megabase euchromatic portion of the Drosophila genome using a whole-genome shotgun sequencing strategy supported by extensive clone-based sequence and a high-quality bacterial artificial chromosome physical map. Efforts are under way to close the remaining gaps; however, the sequence is of sufficient accuracy and contiguity to be declared substantially complete and to support an initial analysis of genome structure and preliminary gene annotation and interpretation. The genome encodes approximately 13,600 genes, somewhat fewer than the smaller Caenorhabditis elegans genome, but with comparable functional diversity.
ESTHER : Adams_2000_Science_287_2185
PubMedSearch : Adams_2000_Science_287_2185
PubMedID: 10731132
Gene_locus related to this paper: drome-1vite , drome-2vite , drome-3vite , drome-a1z6g9 , drome-abhd2 , drome-ACHE , drome-b6idz4 , drome-BEM46 , drome-CG5707 , drome-CG5704 , drome-CG1309 , drome-CG1882 , drome-CG1986 , drome-CG2059 , drome-CG2493 , drome-CG2528 , drome-CG2772 , drome-CG3160 , drome-CG3344 , drome-CG3523 , drome-CG3524 , drome-CG3734 , drome-CG3739 , drome-CG3744 , drome-CG3841 , drome-CG4267 , drome-CG4382 , drome-CG4390 , drome-CG4572 , drome-CG4582 , drome-CG4851 , drome-CG4979 , drome-CG5068 , drome-CG5162 , drome-CG5355 , drome-CG5377 , drome-CG5397 , drome-CG5412 , drome-CG5665 , drome-CG5932 , drome-CG5966 , drome-CG6018 , drome-CG6113 , drome-CG6271 , drome-CG6283 , drome-CG6295 , drome-CG6296 , drome-CG6414 , drome-CG6431 , drome-CG6472 , drome-CG6567 , drome-CG6675 , drome-CG6753 , drome-CG6847 , drome-CG7329 , drome-CG7367 , drome-CG7529 , drome-CG7632 , drome-CG8058 , drome-CG8093 , drome-CG8233 , drome-CG8424 , drome-CG8425 , drome-CG9059 , drome-CG9186 , drome-CG9287 , drome-CG9289 , drome-CG9542 , drome-CG9858 , drome-CG9953 , drome-CG9966 , drome-CG10116 , drome-CG10163 , drome-CG10175 , drome-CG10339 , drome-CG10357 , drome-CG10982 , drome-CG11034 , drome-CG11055 , drome-CG11309 , drome-CG11319 , drome-CG11406 , drome-CG11598 , drome-CG11600 , drome-CG11608 , drome-CG11626 , drome-CG11935 , drome-CG12108 , drome-CG12869 , drome-CG13282 , drome-CG13562 , drome-CG13772 , drome-CG14034 , drome-nlg3 , drome-CG14717 , drome-CG15101 , drome-CG15102 , drome-CG15106 , drome-CG15111 , drome-CG15820 , drome-CG15821 , drome-CG15879 , drome-CG17097 , drome-CG17099 , drome-CG17101 , drome-CG17191 , drome-CG17192 , drome-CG17292 , drome-CG18258 , drome-CG18284 , drome-CG18301 , drome-CG18302 , drome-CG18493 , drome-CG18530 , drome-CG18641 , drome-CG18815 , drome-CG31089 , drome-CG31091 , drome-CG32333 , drome-CG32483 , drome-CG33174 , drome-dnlg1 , drome-este4 , drome-este6 , drome-GH02384 , drome-GH02439 , drome-glita , drome-KRAKEN , drome-lip1 , drome-LIP2 , drome-lip3 , drome-MESK2 , drome-nrtac , drome-OME , drome-q7k274 , drome-Q9VJN0 , drome-Q8IP31 , drome-q9vux3