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138 Newest Publications of Portland Press

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The disease-associated mutation of the mitochondrial sulphydryl oxidase Erv1 impairs cofactor binding during its catalytic reaction

01-10-2014 | Ceh-Pavia E; Ang S; Spiller M; Lu H, Biochemical Journal, 2014

Erv1(essential for respiration and viability 1) is an FAD-dependent sulphydryl oxidase of the Erv/ALR (augmenter of liver regeneration) sub-family. It is an essential component of the mitochondrial import and assembly (MIA) pathway, playing an important role in the oxidative folding of ...

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Chromatin and oxygen sensing in the context of JmjC histone demethylases

15-09-2014 | Shmakova A; Batie M; Druker J; Rocha S, Biochemical Journal, 2014

Responding appropriately to changes in oxygen availability is essential for multicellular organism survival. Molecularly, cells have evolved intricate gene expression programmes to handle this stressful condition. Although it is appreciated that gene expression is co-ordinated by changes in ...

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Mutation of tryptophan 93 of MauG to tyrosine causes loss of bound Ca{Less than}sup{Greater than}2{+}{Less than}/sup{Greater than} and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis

11-09-2013 | Shin S; Feng M; Davidson V, Biochemical Journal, 2013

The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its tryptophan tryptophylquinone (TTQ) cofactor. Trp93 of MauG is positioned midway between its two hemes, ...

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On the catalytic mechanism of dimeric dUTPases

04-09-2013 | Hemsworth G; Gonz{a}lez-Pacanowska D; Wilson K, Biochemical Journal, 2013

The Tritryps Trypanosoma brucei, T. cruzi and Leishmania donovani are responsible for great morbidity and mortality in developing countries. Their dimeric dUTPases are members of the all-a NTP pyrophosphohydrolase family and represent promising drug targets due to their essential nature and ...

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Completing the folate biosynthesis pathway in {Less than}i{Greater than}Plasmodium falciparum{Less than}/i{Greater than}: {Less than}i{Greater than}p{Less than}/i{Greater than}-aminobenzoate is produced by a highly divergent, promiscuous aminodeoxychorismate lyase

19-08-2013 | Magnani G; Lomazzi M; Peracchi A, Biochemical Journal, 2013

Enzymes that produce or recycle folates are the targets of widely used antimalarial drugs. Despite the interest in the folate metabolism in Plasmodium falciparum, the molecular identification of aminodeoxychorismate lyase (ADCL), which synthesizes the p-aminobenzoate moiety of folate, remained ...

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A novel fluorescent assay and catalytic properties of Crh1 and Crh2 yeast cell wall transglycosylases

06-08-2013 | Maz{a}{n} M; Blanco N; Kov{a}{c with caron}ov{a} K; Zemkov{a} Z; {R}ehulka P; Farka{s with caron} V; Arroyo J, Biochemical Journal, 2013

Mechanical properties of fungal cell walls are largely determined by composition and mutual cross-linking of their macromolecular components. Previous work showed that the Crh proteins are required for the formation of cross-links between chitin and glucan at the Saccharomyces cerevisiae cell ...

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Crystal structures of SCP2-thiolases of Trypanosomatidae, human pathogens causing widespread tropical diseases: the importance for catalysis of the cysteine of the unique HDCF loop

02-08-2013 | Harijan R; Kiema T; Karjalainen M; Janardan N; Murthy M; Weiss M; Michels P; Wierenga R, Biochemical Journal, 2013

Thiolases are essential CoA dependent enzymes in lipid metabolism. Here we report on crystal structures of trypanosomal and leishmanial SCP2-thiolases. Trypanosomatidae cause various widespread, devastating (sub)-tropical diseases, for which adequate treatment is lacking. The structures reveal ...

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A cross-kingdom Nudix enzyme that pre-empts damage in thiamin metabolism

09-07-2013 | Goyer A; Hasnain G; Frelin O; Ralat M; Gregory J; Hanson A, Biochemical Journal, 2013

Genes specifying the thiamin monophosphate phosphatase and adenylated thiazole diphosphatase steps in fungal and plant thiamin biosynthesis remain unknown, as do genes for thiamin diphosphate (ThDP) hydrolysis in thiamin metabolism. A distinctive Nudix domain fused to thiamin diphosphokinase ...

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Ube2W conjugates ubiquitin to α-amino groups of protein N-termini

01-07-2013 | Tatham MH; Plechanovova A; Jaffray EG; Salmen H; Hay RT, Biochemical Journal, 2013

The covalent attachment of the protein ubiquitin to intracellular proteins by a process known as ubiquitylation regulates almost all major cellular systems, predominantly by regulating protein turnover. Ubiquitylation requires the co-ordinated action of three enzymes termed E1, E2 and E3, and ...

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The glyoxalase pathway: the first hundred yearsEllipsis and beyond

01-07-2013 | Sousa Silva M; Gomes RA; Ferreira AEN; Ponces Freire A; Cordeiro C, Biochemical Journal, 2013

The discovery of the enzymatic formation of lactic acid from methylglyoxal dates back to 1913 and was believed to be associated with one enzyme termed ketonaldehydemutase or glyoxalase, the latter designation prevailed. However, in 1951 it was shown that two enzymes were needed and that ...

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