Nagura T

References (2)

Title : Ingestion of difructose anhydride III partially suppresses the deconjugation and 7alpha-dehydroxylation of bile acids in rats fed with a cholic acid-supplemented diet - Lee_2019_Biosci.Biotechnol.Biochem__1
Author(s) : Lee DG , Hori S , Kohmoto O , Kitta S , Yoshida R , Tanaka Y , Shimizu H , Takahashi K , Nagura T , Uchino H , Fukiya S , Yokota A , Ishizuka S
Ref : Biosci Biotechnol Biochem , :1 , 2019
Abstract : Difructose anhydride III (DFAIII) is a prebiotic involved in the reduction of secondary bile acids (BAs). We investigated whether DFAIII modulates BA metabolism, including enterohepatic circulation, in the rats fed with a diet supplemented with cholic acid (CA), one of the 12alpha-hydroxylated BAs. After acclimation, the rats were fed with a control diet or a diet supplemented with DFAIII. After 2 weeks, each group was further divided into two groups and was fed diet with or without CA supplementation at 0.5 g/kg diet. BA levels were analyzed in aortic and portal plasma, liver, intestinal content, and feces. As a result, DFAIII ingestion reduced the fecal deoxycholic acid level via the partial suppression of deconjugation and 7alpha-dehydroxylation of BAs following CA supplementation. These results suggest that DFAIII suppresses production of deoxycholic acid in conditions of high concentrations of 12alpha-hydroxylated BAs in enterohepatic circulation, such as obesity or excess energy intake. Abbreviation: BA: bile acid; BSH: bile salt hydrolase; CA: cholic acid; DCA: deoxycholic acid; DFAIII: difructose anhydride III; MCA: muricholic acid; MS: mass spectrometry; NCDs: non-communicable diseases; LC: liquid chromatography; SCFA: short-chain fatty acid; TCA: taurocholic acid; TCDCA: taurochenodeoxycholic acid; TDCA: taurodeoxycholic acid; TUDCA: tauroursodeoxychlic acid; TalphaMCA: tauro-alpha-muricholic acid; TbetaMCA: tauro-beta-muricholic acid; TomegaMCA: tauro-omega-muricholic acid.
ESTHER : Lee_2019_Biosci.Biotechnol.Biochem__1
PubMedSearch : Lee_2019_Biosci.Biotechnol.Biochem__1
PubMedID: 30912732

Title : Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2 - Kodama_2009_Proteins_77_710
Author(s) : Kodama Y , Masaki K , Kondo H , Suzuki M , Tsuda S , Nagura T , Shimba N , Suzuki E , Iefuji H
Ref : Proteins , 77 :710 , 2009
Abstract : The structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity.
ESTHER : Kodama_2009_Proteins_77_710
PubMedSearch : Kodama_2009_Proteins_77_710
PubMedID: 19544571
Gene_locus related to this paper: crysp-Q874E9