Dohmae N

References (4)

Title : Triazole Ureas Covalently Bind to Strigolactone Receptor and Antagonize Strigolactone Responses - Nakamura_2019_Mol.Plant_12_44
Author(s) : Nakamura H , Hirabayashi K , Miyakawa T , Kikuzato K , Hu W , Xu Y , Jiang K , Takahashi I , Niiyama R , Dohmae N , Tanokura M , Asami T
Ref : Mol Plant , 12 :44 , 2019
Abstract : Strigolactones, a class of plant hormones with multiple functions, mediate plant-plant and plant-microorganism communications in the rhizosphere. In this study, we developed potent strigolactone antagonists, which covalently bind to the strigolactone receptor D14, by preparing an array of triazole urea compounds. Using yeast two-hybrid and rice-tillering assays, we identified a triazole urea compound KK094 as a potent inhibitor of strigolactone receptors. Liquid chromatography-tandem mass spectrometry analysis and X-ray crystallography revealed that KK094 was hydrolyzed by D14, and that a reaction product of this degradation covalently binds to the Ser residue of the catalytic triad of D14. Furthermore, we identified two triazole urea compounds KK052 and KK073, whose effects on D14-D53/D14-SLR1 complex formation were opposite due to the absence (KK052) or presence (KK073) of a trifluoromethyl group on their phenyl ring. These results demonstrate that triazole urea compounds are potentially powerful tools for agricultural application and may be useful for the elucidation of the complicated mechanism underlying strigolactone perception.
ESTHER : Nakamura_2019_Mol.Plant_12_44
PubMedSearch : Nakamura_2019_Mol.Plant_12_44
PubMedID: 30391752
Gene_locus related to this paper: orysj-Q10QA5

Title : Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation - Okamoto_2017_Biochem.Biophys.Res.Commun_486_558
Author(s) : Okamoto S , Murano T , Suzuki T , Uematsu S , Niwa Y , Sasazawa Y , Dohmae N , Bujo H , Simizu S
Ref : Biochemical & Biophysical Research Communications , 486 :558 , 2017
Abstract : Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia. LPL has one predicted C-mannosylation site at Trp417. In this study, we demonstrated that LPL is C-mannosylated at Trp417 by mass spectrometry. Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type. These data suggest the importance of C-mannosylation for LPL functions.
ESTHER : Okamoto_2017_Biochem.Biophys.Res.Commun_486_558
PubMedSearch : Okamoto_2017_Biochem.Biophys.Res.Commun_486_558
PubMedID: 28327359
Gene_locus related to this paper: human-LPL

Title : Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family - Sato_1997_J.Biol.Chem_272_2192
Author(s) : Sato T , Aoki J , Nagai Y , Dohmae N , Takio K , Doi T , Arai H , Inoue K
Ref : Journal of Biological Chemistry , 272 :2192 , 1997
Abstract : Rat platelets secrete two types of phospholipases upon stimulation; one is type II phospholipase A2 and the other is serine-phospholipid-selective phospholipase A. In the current study we purified serine-phospholipid-selective phospholipase A and cloned its cDNA. The final preparation, purified from extracellular medium of activated rat platelets, gave a 55-kDa protein band on SDS-polyacrylamide gel electrophoresis. [3H]Diisopropyl fluorophosphate, an inhibitor of the enzyme, labeled the 55-kDa protein, suggesting that this polypeptide possesses active serine residues. The cDNA for the enzyme was cloned from a rat megakaryocyte cDNA library. The predicted 456-amino acid sequence contains a putative short N-terminal signal sequence and a GXSXG sequence, which is a motif of an active serine residue of serine esterase. Amino acid sequence homology analysis revealed that the enzyme shares about 30% homology with mammalian lipases (lipoprotein lipase, hepatic lipase, and pancreatic lipase). Regions surrounding the putative active serine, histidine, and aspartic acid, which may form a "lipase triad," were highly conserved among these enzymes. The recombinant protein, which we expressed in Sf9 insect cells using the baculovirus system, hydrolyzed a fatty acyl residue at the sn-1 position of lysophosphatidylserine and phosphatidylserine, but did not appreciably hydrolyze phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidic acid, and triglyceride. The present enzyme, named phosphatidylserine-phospholipase A1, is the first phospholipase that exclusively hydrolyses the sn-1 position and has a strict head group specificity for the substrate.
ESTHER : Sato_1997_J.Biol.Chem_272_2192
PubMedSearch : Sato_1997_J.Biol.Chem_272_2192
PubMedID: 8999922
Gene_locus related to this paper: human-PLA1A , ratno-P97535

Title : Isolation and characterization of the gene encoding an aminopeptidase involved in the selective toxicity of ascamycin toward Xanthomonas campestris pv. citri - Sudo_1996_Biochem.J_319_99
Author(s) : Sudo T , Shinohara K , Dohmae N , Takio K , Usami R , Horikoshi K , Osada H
Ref : Biochemical Journal , 319 :99 , 1996
Abstract : An aminopeptidase gene named XAP has been isolated from Xanthomonas campestris pv. citri, a plant pathogenic bacterium. The bacterium is one of the rare micro-organisms susceptible to ascamycin, an aminoacyl nucleoside antibiotic that inhibits protein synthesis. Sequence analysis reveals that the gene encodes a 311 amino acid protein with a calculated molecular mass of 35134 Da and approx. 50% identity for amino acids to the proline iminopeptidase from Neisseria gonorrhoeae. The XAP gene product, Xap, expressed in Escherichia coli has proline iminopeptidase activity as well as ascamycin dealanylating activity in vitro.
ESTHER : Sudo_1996_Biochem.J_319_99
PubMedSearch : Sudo_1996_Biochem.J_319_99
PubMedID: 8870654
Gene_locus related to this paper: xanca-impep