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4′-Phosphopantetheine and Coenzyme A Biosynthesis in Plants*
TLDR
The cloning of the four missing genes, purification of the enzymes, and identification of their functions are demonstrated and it is shown that the plant synthetase is not CTP-but ATP-dependent.
Regulation of epidermin biosynthetic genes by EpiQ
TLDR
EpiQ, like other DNA‐binding proteins, was shown to bind strongly to heparin sepharose, and controls epidermin production by transcriptionally activating the epiA promoter, used for transcription of most of the epidermine biosynthetic genes.
Targeting of Nbp1 to the inner nuclear membrane is essential for spindle pole body duplication
TLDR
It is established that Nbp1 is a monotopic membrane protein that is essential for SPB insertion at the inner face of the NE and suggested that the amphipathic α‐helix of NBP1 is important forSPB insertion into the NE from within the nucleus.
Crystal structure of the peptidyl‐cysteine decarboxylase EpiD complexed with a pentapeptide substrate
TLDR
The unusual substrate recognition mode and the type of chemical reaction performed provide insight into a novel family of flavoproteins.
Molecular Characterization of Lantibiotic-synthesizing Enzyme EpiD Reveals a Function for Bacterial Dfp Proteins in Coenzyme A Biosynthesis*
TLDR
It is demonstrated that the N-terminal domain of the Escherichia coli Dfp protein catalyzes the decarboxylation of (R)-4′-phospho-N-pantothenoylcysteine to 4′-Phosphopantetheine, essential for coenzyme A biosynthesis.
Protein engineering of lantibiotics
TLDR
The development of expression systems for the structural lantibiotic genes for nisin A, nisin Z, gallidermin, epidermin and Pep5 are described, and examples of recently produced site-directed mutants of these lantIBiotics are given.
The biosynthesis of the lantibiotics epidermin, gallidermin, Pep5 and epilancin K7
TLDR
LanB and LanC are responsible for the dehydration of the serine and threonine residues to give dehydroalanine and dehydrobutyrine and subsequent addition of cysteine SH-groups to the dehydro amino acids which results in the thioether rings.
Arabidopsis thaliana Flavoprotein AtHAL3a Catalyzes the Decarboxylation of 4′-Phosphopantothenoylcysteine to 4′-Phosphopantetheine, a Key Step in Coenzyme A Biosynthesis*
TLDR
It is demonstrated that AtHAL3a catalyzes the decarboxylation of (R)-4′-phospho-N-pantothenoylcysteine to 4′-Phosphopantetheine, a key step in coenzyme A biosynthesis that is catalyzed in bacteria by the Dfp proteins.
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