Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline (S)-lactate Identifier CHEBI:16651 Charge -1 Formula C3H5O3 InChIKeyhelp_outline JVTAAEKCZFNVCJ-REOHCLBHSA-M SMILEShelp_outline C[C@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 28 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (S)-malate Identifier CHEBI:15589 Charge -2 Formula C4H4O5 InChIKeyhelp_outline BJEPYKJPYRNKOW-REOHCLBHSA-L SMILEShelp_outline O[C@@H](CC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:79475 | RHEA:79476 | RHEA:79477 | RHEA:79478 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Stereoselectivity of the membrane potential-generating citrate and malate transporters of lactic acid bacteria.
Bandell M., Lolkema J.S.
The citrate transporter of Leuconostoc mesenteroides (CitP) and the malate transporter of Lactococcus lactis (MleP) are homologous proteins that catalyze citrate-lactate and malate-lactate exchange, respectively. Both transporters transport a range of substrates that contain the 2-hydroxycarboxyla ... >> More
The citrate transporter of Leuconostoc mesenteroides (CitP) and the malate transporter of Lactococcus lactis (MleP) are homologous proteins that catalyze citrate-lactate and malate-lactate exchange, respectively. Both transporters transport a range of substrates that contain the 2-hydroxycarboxylate motif, HO-CR(2)-COO(-) [Bandell, M., et al. (1997) J. Biol. Chem. 272, 18140-18146]. In this study, we have analyzed binding and translocation properties of CitP and MleP for a wide variety of substrates and substrate analogues. Modification of the OH or the COO(-) groups of the 2-hydroxycarboxylate motif drastically reduced the affinity of the transporters for the substrates, indicating their relevance in substrate recognition. Both CitP and MleP were strictly stereoselective when the R group contained a second carboxylate group; the S-enantiomers were efficiently bound and translocated, while the transporters had no affinity for the R-enantiomers. The affinity of the S-enantiomers, and of citrate, was at least 1 order of magnitude higher than for lactate and other substrates with uncharged R groups, indicating a specific interaction between the second carboxylate group and the protein that is responsible for high-affinity binding. MleP was not stereoselective in binding when the R groups are hydrophobic and as large as a benzyl group. However, only the S-enantiomers were translocated by MleP. CitP had a strong preference for binding and translocating the R-enantiomers of substrates with large hydrophobic R groups. These differences between CitP and MleP explain why citrate is a substrate of CitP and not of MleP. The results are discussed in the context of a model for the interaction between sites on the protein and functional groups on the substrates in the binding pockets of the two proteins. << Less
Biochemistry 38:10352-10360(1999) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.