Enzymes
| UniProtKB help_outline | 1,470 proteins |
Reaction participants Show >> << Hide
- Name help_outline glycolate Identifier CHEBI:29805 (CAS: 666-14-8) help_outline Charge -1 Formula C2H3O3 InChIKeyhelp_outline AEMRFAOFKBGASW-UHFFFAOYSA-M SMILEShelp_outline OCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 24 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:29411 | RHEA:29412 | RHEA:29413 | RHEA:29414 | |
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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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Transport of L-lactate, D-lactate, and glycolate by the LldP and GlcA membrane carriers of Escherichia coli.
Nunez M.F., Kwon O., Wilson T.H., Aguilar J., Baldoma L., Lin E.C.C.
To examine the substrate specificity of the membrane transport carriers LldP (L-lactate permease) and GlcA (glycolate permease) of Escherichia coli, a mutant strain lacking their structural genes and blocked in the metabolism of the tested substrates was constructed and transformed with a plasmid ... >> More
To examine the substrate specificity of the membrane transport carriers LldP (L-lactate permease) and GlcA (glycolate permease) of Escherichia coli, a mutant strain lacking their structural genes and blocked in the metabolism of the tested substrates was constructed and transformed with a plasmid bearing either the lldP or the glcA gene. Each transformant acquired the ability to accumulate L-lactate, D-lactate, and glycolate against a high concentration gradient. Substrate accumulation was inhibited by carbonyl cyanide m-chlorophenylhydrazone, a hydrophobic proton conductor that dissipates proton motive force. Competition of (14)C-L-lactate transport by nonradioactive L-lactate, D-lactate, and glycolate in LldP synthesizing cells and competition of (14)C-glycolate transport by the same three substrates in GlcA synthesizing cells showed that both carriers effectively transported all three substrates with a K(i) value ranging from 10 to 20 microM. D-Lactate does not appear to have a permease of its own. Utilization of the compound depends mainly on LldP. << Less
Biochem. Biophys. Res. Commun. 290:824-829(2002) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.