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A new enzyme superfamily - the phosphopantetheinyl transferases.
TLDR
This work has identified a large family of proteins having 12-22 % similarity with ACPS, which are putative P-pant transferases, and found three of these proteins, E. coli EntD and o195, and subtilis Sfp, have been overproduced, purified and found to have P- pant transferase activity.
Iron acquisition in plague: modular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis.
TLDR
Sequence analysis of yersiniabactin biosynthetic regions reveals a strategy for siderophore production using a mixed polyketide synthase/nonribosomal peptide synthetase complex formed between HMWP1 and H MWP2 (encoded by irp1 and irp2).
Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5.
TLDR
The Lys5/Lys2 pair is identified as a two-component system in which Lys5 covalently primes Lys2, allowing alpha-aminoadipate reductase activity by holo-Lys1 with catalytic cycles of autoaminoacylation and reductive cleavage.
Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF.
TLDR
The first reconstitution of enterobactin synthetase activity from pure protein components: hol-EntB, EntE, and holo-EntF is reported, thereby eliminating the requirement for EntD in the enterobactsin Synthetase.
Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and
TLDR
It is shown that EntB, previously described as the isochorismate lyase required for production of 2,3-DHB, is a bifunctional protein that also serves as an aryl carrier protein (ArCP) with a role in enterobactin assembly.
Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
TLDR
Kinetic studies demonstrated that a pre-steady-state lag in the production of UDP-N-acetylglucosamine from acetyl-CoA, UTP, and glucosamine-1-P was due to the release and accumulation of steady-state levels of the intermediate N-acetelglucOSamine- 1-P.
Post-translational modification of polyketide and nonribosomal peptide synthases.
TLDR
Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantethinyl transfer.
Identification and Characterization of Bacterial Cysteine Dioxygenases: a New Route of Cysteine Degradation for Eubacteria
TLDR
Kinetic data strongly indicate that four proteins from Bacillus subtilis, Bacillus cereus, and Streptomyces coelicolor A3(2) that shared low overall identity to CDO but nevertheless conserved important active-site residues are indeed bona fide CDOs and suggest that a large subset of eubacteria is capable of cysteine sulfoxidation.
The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis.
TLDR
This work provides the first biochemical evidence for the role of the Yersinia pestis high molecular weight protein 2 (HMWP2), a nonribosomal peptide synthetase homologue, and YbtE in the initiation of yersiniabactin biosynthesis.
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