Literature DB >> 26875494

Purification and Properties of Glycine Oxidase from Pseudomonas putida KT2440.

Messele Yohannes Equar1, Yasushi Tani, Hisaaki Mihara.   

Abstract

Glycine oxidase, encoded by the thiO gene, participates in the biosynthesis of thiamin by providing glyoxyl imine to form the thiazole moiety of thiamin. We have purified and characterized ThiO from Pseudomonas putida KT2440. It has a monomeric structure that is distinct from the homotetrameric ThiOs from Bacillus subtilis and Geobacillus kaustophilus. The P. putida ThiO is unique in that glycine is its preferred substrate, which differs markedly from the B. subtilis and G. kaustophilus enzymes that use D-proline as the preferred substrate.

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Year:  2015        PMID: 26875494     DOI: 10.3177/jnsv.61.506

Source DB:  PubMed          Journal:  J Nutr Sci Vitaminol (Tokyo)        ISSN: 0301-4800            Impact factor:   2.000


  2 in total

1.  Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea.

Authors:  Andres Andreo-Vidal; Kyle J Mamounis; Esha Sehanobish; Dante Avalos; Jonatan Cristian Campillo-Brocal; Antonio Sanchez-Amat; Erik T Yukl; Victor L Davidson
Journal:  Biochemistry       Date:  2018-02-06       Impact factor: 3.162

2.  Phylogeny resolved, metabolism revealed: functional radiation within a widespread and divergent clade of sponge symbionts.

Authors:  Jessica A Taylor; Giorgia Palladino; Bernd Wemheuer; Georg Steinert; Detmer Sipkema; Timothy J Williams; Torsten Thomas
Journal:  ISME J       Date:  2020-10-03       Impact factor: 10.302

  2 in total

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