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Gene Review:

prpD - 2-methylcitrate dehydratase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0331, JW0325, acnC, yahT

Lee, S.K. et al., Blank, L. et al., Horswill, A.R. et al., Gulick, A.M. et al., Horswill, A.R. et al., et al.

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Disease relevance of prpD

These compounds have been used to crystallize an enzyme encoded by the Salmonella enterica prpD gene that catalyzes the dehydration of 2-methylcitrate to form 2-methyl-cis-aconitate [1].
In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate [2].
AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates [3].

High impact information on prpD

This work shows that the prpD gene of the prpBCDE operon of this bacterium encodes a protein with 2-methylcitrate dehydratase enzyme activity [2].
The prpD(-) strain exhibited low expression in the presence of glucose, highly regulatable expression over a wide range of propionate concentrations, and, in contrast to the wild-type strain, fast induction to full expression under all growth conditions [4].
The expression and regulatory properties of a propionate-regulated overexpression system (Salmonella enterica prpBCDE promoter (P(prpB)) and positive regulator (prpR)) were evaluated in wild-type S. enterica serovar Typhimurium TR6583 and prpB(-) or prpD(-) versions of this strain and compared with the arabinose-regulated T7 expression system [4].
The reactions are catalyzed by propionyl coenzyme A (propionyl-CoA) synthetase (PrpE), 2-methylcitrate synthase (PrpC), 2-methylcitrate dehydratase (probably PrpD), 2-methylisocitrate hydratase (probably PrpD), and 2-methylisocitrate lyase (PrpB) [5].
Inactivation of prpD abolished the residual aconitase activity of an AcnAB-null strain, whereas inactivation of ybhJ, an unidentified acnA paralogue, had no significant effect on AcnC activity [3].

Biological context of prpD

Finally, we report the location of MudI1734 elements inserted in prpC or prpD and of a Tn10delta16delta17 element in prpB and provide genetic evidence supporting the conclusion that the prpBCDE genes constitute an operon [6].

Associations of prpD with chemical compounds

Here it is shown that a 2-methylcitrate dehydratase (PrpD) encoded by the prpD gene of the propionate catabolic operon (prpRBCDE) is identical to AcnC [3].
Pentaerythritol propoxylate: a new crystallization agent and cryoprotectant induces crystal growth of 2-methylcitrate dehydratase [1].

References

Pentaerythritol propoxylate: a new crystallization agent and cryoprotectant induces crystal growth of 2-methylcitrate dehydratase. Gulick, A.M., Horswill, A.R., Thoden, J.B., Escalante-Semerena, J.C., Rayment, I. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate. Horswill, A.R., Escalante-Semerena, J.C. Biochemistry (2001) [Pubmed]
AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates. Blank, L., Green, J., Guest, J.R. Microbiology (Reading, Engl.) (2002) [Pubmed]
A Salmonella-based, propionate-inducible, expression system for Salmonella enterica. Lee, S.K., Keasling, J.D. Gene (2006) [Pubmed]
Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. Horswill, A.R., Escalante-Semerena, J.C. J. Bacteriol. (1999) [Pubmed]
Propionate catabolism in Salmonella typhimurium LT2: two divergently transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a member of the sigma-54 family of activators, and the prpBCDE genes constitute an operon. Horswill, A.R., Escalante-Semerena, J.C. J. Bacteriol. (1997) [Pubmed]

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