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Volume 139, Issue 7

Identification of the L-tartrate dehydratase genes ( and ) of and evolutionary relationship with the Class I fumarase genes Free

Abstract

Summary: The genes encoding an oxygen-labile stereospecific L-tartrate dehydratase (L-Ttd, EC 4.2.1.32) have been identified as the and genes located upstream of the operon at 67 min in the linkage map. They were previously cloned and sequenced by M. Nesin and others ( 51, 149-161, 1987) and have now been independently cloned, partially resequenced, and designated as an operon () containing two translationally coupled genes. The enzyme behaves as a tetramer (Mr 105000) containing two pairs of non-identical subunits, TtdA (M 32589) and TtdB (M 22641), which otherwise resembles the homodimerie iron-sulphur-containing Class I fumarases of and The amino acid sequences of the TtdA-TtdB subunits are colinearly related to a single fumarase subunit, indicating a common evolutionary ancestry. can use L-, D- and -tsrtrates as aerobic growth substrates and as reducible substrates for supporting anaerobic growth on glycerol. L-Ttd was induced during anaerobic growth on glycerol plus L- and -tartrates, and a stereospecific D-tartrate dehydratase was induced by all three stereoisomers under comparable conditions. No -tartrate dehydratase was detected, nor were any dehydratases detected after aerobic growth on tartrate minimal media suggesting that different catabolic routes operate under aerobic conditions.

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  • Published Online:
© Society for General Microbiology 1993
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1993-07-01
2024-04-25
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Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the Class I fumarase genes
Microbiology 139, 1523 (1993); https://doi.org/10.1099/00221287-139-7-1523
/content/journal/micro/10.1099/00221287-139-7-1523
/content/journal/micro/10.1099/00221287-139-7-1523
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