A thermodynamic study of the conversion of chorismate to isochorismate

Tewari, Yadu B.; Davis, Andrew M.; Reddy, P.G.; Goldberg, Robert N.

doi:10.1006/jcht.2000.0677

Cited by 7 publications

(6 citation statements)

References 22 publications

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“…Detection was carried out at 280 nm. (30) was generated by the reaction of chorismate with the isochorismate synthase EntC. EntC was then removed by ultrafiltration.…”

Section: Methodsmentioning

confidence: 99%

Salicylate Biosynthesis: Overexpression, Purification, and Characterization of Irp9, a Bifunctional Salicylate Synthase fromYersinia enterocolitica

et al. 2005

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In some bacteria, salicylate is synthesized using the enzymes isochorismate synthase and isochorismate pyruvate lyase. In contrast, gene inactivation and complementation experiments with Yersinia enterocolitica suggest the synthesis of salicylate in the biosynthesis of the siderophore yersiniabactin involves a single protein, Irp9, which converts chorismate directly into salicylate. In the present study, Irp9 was for the first time heterologously expressed in Escherichia coli as a hexahistidine fusion protein, purified to near homogeneity, and characterized biochemically. The recombinant protein was found to be a dimer, each subunit of which has a molecular mass of 50 kDa. Enzyme assays, reverse-phase high-pressure liquid chromatography and 1 H nuclear magnetic resonance (NMR) spectroscopic analyses confirmed that Irp9 is a salicylate synthase and converts chorismate to salicylate with a K m for chorismate of 4.2 M and a k cat of 8 min ؊1 . The reaction was shown to proceed through the intermediate isochorismate, which was detected directly using 1 H NMR spectroscopy.

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“…Detection was carried out at 280 nm. (30) was generated by the reaction of chorismate with the isochorismate synthase EntC. EntC was then removed by ultrafiltration.…”

Section: Methodsmentioning

confidence: 99%

Salicylate Biosynthesis: Overexpression, Purification, and Characterization of Irp9, a Bifunctional Salicylate Synthase fromYersinia enterocolitica

et al. 2005

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“…Microorganisms do not usually possess both type II and type I DAHP synthases and this represents the first report of such a case. One of the type II DAHP isozymes was found to play a role in the biosynthetic pathway to the family of electron transport inhibitors called the aurachins (see aurachin A 13) known to derive from anthranilate (12) and acetate.…”

Section: Dahp Synthasementioning

confidence: 99%

The biosynthesis of shikimate metabolites

Knaggs

2002

Nat. Prod. Rep.

178

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This review covers the literature published during 2000 on the biosynthesis of compounds derived wholly or partly from intermediates on the shikimate pathway. Recent developments in the enzymology and genetics of the shikimate pathway arc also described. Enzymes involved in the biogenetic pathway to the aromatic amino acids are covered initially followed by sections dedicated to metabolites derived in some part from intermediates on the pathway. These include pyrrolnitrin. violacein. indole-3-acetic acid, coumarins, lignans, lignin, tannins, melanin, flavanoids, ubiquinone, TOPA quinone, PQQ, and tropanes.

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“…27 The molar enthalpy of the reaction from chorismate to isochorismate in solution was determined as D r H m ¼ Àð0:81 AE 0:27Þ kJ mol À1 by the Goldberg group. 28 1.1.2. Enzymatic reactions of chorismate and isochorismate.…”

Section: Introductionmentioning

confidence: 99%