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<< < Results 11 - 20 of 117 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2759218 Phylogeny and foraging mode correspond with thiaminase activity in freshwater fishes Potential links to environmental factors Freshw. Sci. 38 605-615 2019 Dorosoma cepedianum -
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2758667 Thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis Appl. Environ. Microbiol. 84 e01268-18 2018 Burkholderia thailandensis 30006396
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2758667 Thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis Appl. Environ. Microbiol. 84 e01268-18 2018 Burkholderia thailandensis ATCC 700388 30006396
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2739509 A rapid method for assaying thiaminase I activity in diverse biological samples PLoS ONE 9 e92688 2014 Paenibacillus thiaminolyticus 24675843
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2739509 A rapid method for assaying thiaminase I activity in diverse biological samples PLoS ONE 9 e92688 2014 Paenibacillus thiaminolyticus 8103 24675843
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2684401 An assay for thiaminase I in complex biological samples Anal. Biochem. 368 33-38 2007 Paenibacillus thiaminolyticus 17603991
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2636858 Crystallization and preliminary x-ray analysis of thiaminase I from Bacillus thiaminolyticus: space group change upon freezing of crystals Acta Crystallogr. Sect. D 54 448-450 1998 Paenibacillus thiaminolyticus 9761925
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2636854 Identification of modification sites in large biomolecules by stable isotope labeling and tandem high resolution mass spectrometry. The active site nucleophile of thiaminase I J. Biol. Chem. 272 32215-32220 1997 Paenibacillus thiaminolyticus 9405424
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2636852 Inhibition of thiaminase I from Bacillus thiaminolyticus. Evidence supporting a covalent 1,6-dihydropyrimidinyl-enzyme intermediate Biochemistry 26 1969-1973 1987 Paenibacillus thiaminolyticus 3593702
Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.2636852 Inhibition of thiaminase I from Bacillus thiaminolyticus. Evidence supporting a covalent 1,6-dihydropyrimidinyl-enzyme intermediate Biochemistry 26 1969-1973 1987 Paenibacillus thiaminolyticus BMM 3593702
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