In Escherichia coli , 1-deoxy- d -xylulose (or its 5-phosphate, DXP) is the biosynthetic precursor to isopentenyl diphosphate [Broers, S. T. J. (1994) Dissertation (Eidgenössische Technische Hochschule, Zürich)], thiamin, and pyridoxol [Himmeldirk, K., Kennedy, I. A., Hill, R. E., Sayer, B. G. & Spenser, D. (1996) Chem. Commun . 1187–1188]. Here we show that an open reading frame at 9 min on chromosomal map of E. encodes enzyme ( eoxy x ylulose-5- p hosphate synthase, DXP synthase)...

The structural characterization of proteins expressed from the genome is a major problem in proteomics. solution to this requires separation protein interest complex mixture, identification its DNA-predicted sequence, and sequencing errors posttranslational modifications. For this, "top down" mass spectrometry (MS) approach, extended by greatly increased fragmentation electron capture dissociation (ECD), has been applied characterize involved biosynthesis thiamin, Coenzyme A, hydroxylation...

Background Thioredoxin participates in thiol–disulfide exchange reactions and both oxidized thio redoxin (disulfide form) reduced thioredoxin (dithiol are foundunder physiological conditions. Previous structural studies suggested that the two forms were extremely similar, although significant functional spectroscopic differences exist. We therefore undertook high-resolution solution of Escherichia coli order to detect subtle conformational differences.Results The structures similar. Backbone...

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPhenoxazinone synthase: mechanism for the formation of phenoxazinone chromophore actinomycinClifton E. Barry, III, Parmesh G. Nayar, and Tadhg P. BegleyCite this: Biochemistry 1989, 28, 15, 6323–6333Publication Date (Print):July 25, 1989Publication History Published online1 May 2002Published inissue 25 July 1989https://pubs.acs.org/doi/10.1021/bi00441a026https://doi.org/10.1021/bi00441a026research-articleACS PublicationsRequest reuse...

Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible for the oxidation of cysteine with molecular oxygen to form sulfinate. This reaction commits either catabolism sulfate and pyruvate or taurine biosynthetic pathway. member cupin superfamily proteins. The crystal structure recombinant rat has been determined 1.5-Å resolution, these results confirm canonical β-sandwich fold rare cysteinyltyrosine intramolecular cross-link (between Cys93 Tyr157) seen in recently reported...

Significance Vitamin B 12 is required by humans and a variety of other organisms for diverse metabolic processes, but produced only subset microorganisms. The anaerobic biosynthesis the “lower ligand” , 5,6-dimethylbenzimidazole (DMB), unknown component biosynthetic pathway. We report identification bzaABCDE genes that are necessary sufficient DMB. have characterized role each bza identified three intermediates in This finding not completes pathway also enables sequence-based prediction...

The crystal structure of Bacillus subtilis orotidine 5′-monophosphate (OMP) decarboxylase with bound uridine has been determined by multiple wavelength anomalous diffraction phasing techniques and refined to an R -factor 19.3% at 2.4 Å resolution. OMP is a dimer two identical subunits. Each monomer consists triosephosphate isomerase barrel contains active site that located across one end the near interface. For each site, most residues are contributed few from adjacent monomer. highly...

ThiFSGH and ThiI are required for the biosynthesis of thiazole moiety thiamin in Escherichia coli. The overproduction, purification, characterization ThiFS identification two early steps described here. ThiS isolated from E. coli thiI+ is post-translationally modified by converting carboxylic acid group carboxyl-terminal glycine into a thiocarboxylate. ThethiI gene plays an essential role formation thiocarboxylate because athiI− strain does not contain this modification. ThiF catalyzes...

Oxalate decarboxylase is a manganese-dependent enzyme that catalyzes the conversion of oxalate to formate and carbon dioxide. We have determined structure from Bacillus subtilis at 1.75 A resolution in presence formate. The reveals hexamer with 32-point symmetry which each monomer belongs cupin family proteins. further classified as bicupin because it contains two folds, possibly resulting gene duplication. Each domain one manganese binding site. domains structurally similar oxidase,...

While most of the proteins required for biosynthesis thiamin pyrophosphate have been known more than a decade, reconstitution this in defined biochemical system has difficult due to novelty chemistry involved. Here we demonstrate first successful enzymatic synthesis thiazole moiety from glycine, cysteine, and deoxy-d-xylulose-5-phosphate using overexpressed Bacillus subtilis ThiF, ThiS, ThiO, ThiG, NifS-like protein. This facilitated identification function each involved: ThiF catalyzes...

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPhotoenzymes: A Novel Class of Biological CatalystsTadhg P. BegleyCite this: Acc. Chem. Res. 1994, 27, 12, 394–401Publication Date (Print):December 1, 1994Publication History Published online1 May 2002Published inissue 1 December 1994https://pubs.acs.org/doi/10.1021/ar00048a002https://doi.org/10.1021/ar00048a002research-articleACS PublicationsRequest reuse permissionsArticle Views693Altmetric-Citations119LEARN ABOUT THESE METRICSArticle Views are...

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPhenoxazinone synthase: enzymatic catalysis of an aminophenol oxidative cascadeClifton E. Barry, Parmesh G. Nayar, and Tadhg P. BegleyCite this: J. Am. Chem. Soc. 1988, 110, 10, 3333–3334Publication Date (Print):May 1, 1988Publication History Published online1 May 2002Published inissue 1 1988https://pubs.acs.org/doi/10.1021/ja00218a072https://doi.org/10.1021/ja00218a072research-articleACS PublicationsRequest reuse permissionsArticle...

The structure of tryptophan 2,3-dioxygenase (TDO) from Ralstonia metallidurans was determined at 2.4 Å. TDO catalyzes the irreversible oxidation l-tryptophan to N-formyl kynurenine, which is initial step in catabolism. a heme-containing enzyme and highly specific for its substrate l-tryptophan. tetramer with heme cofactor bound each active site. monomeric fold, as well binding site, similar that large domain indoleamine 2,3-dioxygenase, an same reaction except broader tolerance. Modeling...

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial lyaseTadhg P. Begley, Alan E. Walts, and Christopher T. WalshCite this: Biochemistry 1986, 25, 22, 7192–7200Publication Date (Print):November 4, 1986Publication History Published online1 May 2002Published inissue 4 November 1986https://pubs.acs.org/doi/10.1021/bi00370a064https://doi.org/10.1021/bi00370a064research-articleACS PublicationsRequest reuse permissionsArticle...