Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis.

doi:10.1128/JB.185.16.4837-4843.2003

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Article

Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis.

Journal of bacteriology - 1 Aug 2003

Grimek T L, Holden H, Rayment I, Escalante-Semerena J C

Abstract excerpt

The prpB gene of Salmonella enterica serovar Typhimurium LT2 encodes a protein with 2-methylisocitrate (2-MIC) lyase activity, which cleaves 2-MIC into pyruvate and succinate during the conversion of propionate to pyruvate via the 2-methylcitric acid cycle. This paper reports the isolation and kinetic characterization of wild-type and five mutant PrpB proteins. Wild-type PrpB protein had a molecular mass of...

Topics

Amino Acid Sequence
Bacterial Proteins
Binding Sites
Carbon-Carbon Lyases
Isocitrates
Kinetics
Molecular Sequence Data
Mutation
Salmonella typhimurium
Substrate Specificity

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Identifiers

PMID: 12897003
DOI: 10.1128/JB.185.16.4837-4843.2003
PMCID: PMC166468

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