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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/11/07 15:44:20」(JST)

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Thiamine pyrophosphatase is an enzyme which cleaves thiamine pyrophosphate.

References

Sano S, Matsuda Y, Nakagawa H (1988). "Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase". J Biochem (Tokyo) 103 (4): 678–81. PMID 2844741.

External links

Thiamine pyrophosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Testicular effects of monensin, a golgi interfering agent in male rats.

Singh M, Kalla NR, Sanyal SN.Author information Department of Biophysics, Panjab University , Chandigarh , India.AbstractAbstract Objective: The present study was undertaken to explore the effects of monensin, a potent Golgi disturbing agent on male fertility. Methods: Male Wistar rats were administered monensin at the dose levels of 2.5, 5, and 10 mg/kg b wt. Animals were sacrificed after 67 days of the treatment. The activities of lactate dehydrogenase (LDH), ATPase, acid phosphatase and thiamine pyrophosphatase (TPPase) were measured in the testis. Cytochemical assay of Golgi body marker enzyme, thiamine pyrophosphatase was also performed. Ultrastructural changes in testis were studied by Transmission electron microscopy. Sperm number and motility were also examined. Results and discussion: The alterations in the activities of above mentioned enzymes indicate the pronounced effect of the drug on the functioning of spermatogenic cells. The findings from electron microscopy such as membrane disruption, swelling and disintegration of Golgi apparatus strongly suggest the interference of monensin with the functioning of Golgi apparatus in the spermatogenic cells. Data from the sperm number and motility as well as the fertility studies and the resulted litter size further points towards the antifertility effects of monensin in male rats. Conclusion: The findings from the present study strongly indicated the effects of monensin on the testis, involving alterations in key enzyme activities and changes at the ultrastructural level.
Drug and chemical toxicology.Drug Chem Toxicol.2013 Dec 16. [Epub ahead of print]
Abstract Objective: The present study was undertaken to explore the effects of monensin, a potent Golgi disturbing agent on male fertility. Methods: Male Wistar rats were administered monensin at the dose levels of 2.5, 5, and 10 mg/kg b wt. Animals were sacrificed after 67 days of the treatment.
PMID 24341700

The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.

Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV.Author information Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.AbstractTreponema pallidum, an obligate parasite of humans and the causative agent of syphilis, has evolved the capacity to exploit host-derived metabolites for its survival. Flavin-containing compounds are essential cofactors that are required for metabolic processes in all living organisms, and riboflavin is a direct precursor of the cofactors FMN and FAD. Unlike many pathogenic bacteria, Treponema pallidum cannot synthesize riboflavin; we recently described a flavin-uptake mechanism composed of an ABC-type transporter. However, there is a paucity of information about flavin utilization in bacterial periplasms. Using a discovery-driven approach, we have identified the TP0796 lipoprotein as a previously uncharacterized Mg(2+)-dependent FAD pyrophosphatase within the ApbE superfamily. TP0796 probably plays a central role in flavin turnover by hydrolyzing exogenously acquired FAD, yielding AMP and FMN. Biochemical and structural investigations revealed that the enzyme has a unique bimetal Mg(2+) catalytic center. Furthermore, the pyrophosphatase activity is product-inhibited by AMP, indicating a possible role for this molecule in modulating FMN and FAD levels in the treponemal periplasm. The ApbE superfamily was previously thought to be involved in thiamine biosynthesis, but our characterization of TP0796 prompts a renaming of this superfamily as a periplasmic flavin-trafficking protein (Ftp). TP0796 is the first structurally and biochemically characterized FAD pyrophosphate enzyme in bacteria. This new paradigm for a bacterial flavin utilization pathway may prove to be useful for future inhibitor design.
The Journal of biological chemistry.J Biol Chem.2013 Apr 19;288(16):11106-21. doi: 10.1074/jbc.M113.449975. Epub 2013 Feb 27.
Treponema pallidum, an obligate parasite of humans and the causative agent of syphilis, has evolved the capacity to exploit host-derived metabolites for its survival. Flavin-containing compounds are essential cofactors that are required for metabolic processes in all living organisms, and riboflavin
PMID 23447540

S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.

Chi BK, Roberts AA, Huyen TT, Bäsell K, Becher D, Albrecht D, Hamilton CJ, Antelmann H.Author information Institute for Microbiology, Ernst-Moritz-Arndt-University of Greifswald, Greifswald, Germany.AbstractAIMS: Protein S-bacillithiolations are mixed disulfides between protein thiols and the bacillithiol (BSH) redox buffer that occur in response to NaOCl in Bacillus subtilis. We used BSH-specific immunoblots, shotgun liquid chromatography (LC)-tandem mass spectrometry (MS/MS) analysis and redox proteomics to characterize the S-bacillithiolomes of B. subtilis, B. megaterium, B. pumilus, B. amyloliquefaciens, and Staphylococcus carnosus and also measured the BSH/oxidized bacillithiol disulfide (BSSB) redox ratio after NaOCl stress.
Antioxidants & redox signaling.Antioxid Redox Signal.2013 Apr 10;18(11):1273-95. doi: 10.1089/ars.2012.4686. Epub 2012 Oct 18.
AIMS: Protein S-bacillithiolations are mixed disulfides between protein thiols and the bacillithiol (BSH) redox buffer that occur in response to NaOCl in Bacillus subtilis. We used BSH-specific immunoblots, shotgun liquid chromatography (LC)-tandem mass spectrometry (MS/MS) analysis and redox proteo
PMID 22938038

Japanese Journal

単細胞藻類を用いたゴルジ体系の解析:- Brefeldin Aがゴルジ体系に及ぼす影響-

PLANT MORPHOLOGY 13(1), 51-60, 2001
NAID 130004303764

Three-dimensional Dynamics of the Golgi Apparatus of Parotid Acinar Cells as Analyzed by Computer Graphics of Cytochemically-marked Serial Sections (<Symposium X>Enzyme Cytochemistry : Recent Advances and Applications)

Acta histochemica et cytochemica 32(3), 243-252, 1999
NAID 110003147006

Three-dimensional Dynamics of the Golgi Apparatus in Mitotic Parotid Acinar Cells: Computer-aided Reconstruction from Cytochemically-marked Ultrathin Serial Sections.