The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli

Dahm, Claudia; Müller, Rolf; Schulte, Gaby; Schmidt, Karsten; Leistner, Eckhard

doi:10.1016/s0304-4165(98)00089-0

Cited by 35 publications

(29 citation statements)

References 32 publications

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“…MenF is induced only during anoxygenic conditions. Due to this tight regulation, the two ICS genes show low redundancy (Dahm et al, 1998;Buss et al, 2001). A somewhat different situation has been described for Bacillus subtilis, where one of the two ICS genes can provide isochorismate for dihydroxybenzoate and menaquinone production, but the other one is active only in menaquinone synthesis (Rowland and Taber, 1996).…”

Section: Discussionmentioning

confidence: 94%

Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis

et al. 2008

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Section: Discussionmentioning

confidence: 94%

Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis

et al. 2008

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“…They share a glutamine amidotransferase (GATase) domain in the N-terminal part of the polypeptides, shown by structural data as well as the sequence similarity (Kim et al 1996). (Dahm et al 1998). The pairs of MenF with PabB or TrpE were therefore placed into the fourth section of Table 3 because the reaction chemistries for these pairs are not similar.…”

Section: Genome Research 1377mentioning

confidence: 99%

Divergence of Function in Sequence-Related Groups of Escherichia coli Proteins

Nahum

Riley²

2001

Genome Res.

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The most prominent mechanism of molecular evolution is believed to have been duplication and divergence of genes. Proteins that belong to sequence-related groups in any one organism are candidates to have emerged from such a process and to share a common ancestor. Groups of proteins in Escherichia coli having sequence similarity are mostly composed of proteins with closely related function, but some groups comprise proteins with unrelated functions. In order to understand how function can change while sequences remain similar, we have examined some of these groups in detail. The enzymes analyzed in this work include representatives of amidotransferases, phosphotransferases, decarboxylases, and others. Most sequence-related groups contain enzymes that are in the same classes of Enzyme Commission (EC) numbers. We have concentrated on groups that are heterogeneous in that respect, and also on groups containing more than one enzyme of any pathway. We find that although the EC number may differ, the reaction chemistry of these sequence-related proteins is the same or very similar. Some of these families illustrate how diversification has taken place in evolution, using common features of either reaction chemistry or ligand specificity, or both, to create catalysts for different kinds of biochemical reactions. This information has relevance to the area of functional genomics in which the activities of gene products of unknown reading frames are attributed by analogy to the functions of sequence-related proteins of known function.Groups of sequence-related proteins of Escherichia coli have been assembled that seem likely to have arisen by duplication and divergence of genes in the ancestral genomes, some arising recently, some in early evolutionary times Riley 1995, 1999;Riley and Labedan 1997). Most of the groups are composed of proteins that all have the same reaction chemistry but differ by substrate specificity. Examples are groups of similar-sequence kinase enzymes that act on different substrates, groups of sequence-related acyltransferases that act on different substrates, sets of transcriptional regulators with similar reaction chemistry, and sets of transport proteins that use the same type of mechanism. These and other similar examples are likely to be instances of duplication in which the progeny proteins maintain the reaction chemistry performed, but change the identity of the specific substrate or ligand.However, there are a few examples of sets of sequencerelated enzymes within E. coli that one would not a priori expect to be related: those that seem to catalyze different reactions and those that occur within the same pathway. We collected such examples from among all sequence-related groups or paralogs (for definition, see Fitch 1970) in the E. coli genome (P. Liang, B. Labedan, and M. Riley, in prep.) to find out the biochemical basis of the observed sequence similarity. We found that in the pairs of proteins selected there are examples of (1) similar reaction chemistry but different substrate/ligand sp...

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“…thases (EC 5.4.99.6) catalyze the reversible conversion of chorismate to IC, 3 thereby controlling chorismate partitioning to IC-derived products. Although synthesis and regulation of the bacterial IC pathways have been investigated, there is limited knowledge regarding these enzymes, their products, and their functional roles in plants.…”

mentioning

confidence: 99%

“…In bacteria, ICS enzymes have been associated with either the synthesis of low molecular weight Fe 3ϩ chelators (siderophores) or menaquinones that function as electron acceptors. For example, Escherichia coli contains two ICS genes located in distinct operons encoding proteins with distinct biochemical properties: EntC is expressed under iron-limited conditions and associated with siderophore biosynthesis, and MenF is required for menaquinone biosynthesis and expressed under anaerobic conditions where it plays an essential role in anaerobic electron transport (2)(3)(4)(5). The initial steps in bacterial siderophore production from IC involve the synthesis of salicylic acid (2-hydroxybenzoic acid) or 2,3-dihydroxybenzoic acid; these compounds are then incorporated into siderophores such as pyochelin (Pseudomonas aeruginosa (6)) or enterobactin (E. coli (7)), respectively.…”

mentioning

confidence: 99%

Arabidopsis Isochorismate Synthase Functional in Pathogen-induced Salicylate Biosynthesis Exhibits Properties Consistent with a Role in Diverse Stress Responses

Strawn

Marr

Inoue

et al. 2007

Journal of Biological Chemistry

220

146

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Salicylic acid (SA) is a phytohormone best known for its role in plant defense. It is synthesized in response to diverse pathogens and responsible for the large scale transcriptional induction of defense-related genes and the establishment of systemic acquired resistance. Surprisingly, given its importance in plant defense, an understanding of the underlying enzymology is lacking. In Arabidopsis thaliana, the pathogen-induced accumulation of SA requires isochorismate synthase (AtICS1). Here, we show that AtICS1 is a plastid-localized, stromal protein using chloroplast import assays and immunolocalization. AtICS1 acts as a monofunctional isochorismate synthase (ICS), catalyzing the conversion of chorismate to isochorismate (IC) in a reaction that operates near equilibrium (K eq ‫؍‬ 0.89). It does not convert chorismate directly to SA (via an IC intermediate) as does Yersinia enterocolitica Irp9. Using an irreversible coupled spectrophotometric assay, we found that AtICS1 exhibits an apparent K m of 41.5 M and k cat ‫؍‬ 38.7 min ؊1 for chorismate. This affinity for chorismate would allow it to successfully compete with other pathogen-induced, chorismate-utilizing enzymes. Furthermore, the biochemical properties of AtICS1 indicate its activity is not regulated by light-dependent changes in stromal pH, Mg 2؉ , or redox and that it is remarkably active at 4°C consistent with a role for SA in cold-tolerant growth. Finally, our analyses support plastidic synthesis of stress-induced SA with the requirement for one or more additional enzymes responsible for the conversion of IC to SA, because non-enzymatic conversion of IC to SA under physiological conditions was negligible.

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The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli

Cited by 35 publications

References 32 publications

Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis

Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis

Divergence of Function in Sequence-Related Groups of Escherichia coli Proteins

Arabidopsis Isochorismate Synthase Functional in Pathogen-induced Salicylate Biosynthesis Exhibits Properties Consistent with a Role in Diverse Stress Responses

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