Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
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 O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,727 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetate Identifier CHEBI:30089 (CAS: 71-50-1) help_outline Charge -1 Formula C2H3O2 InChIKeyhelp_outline QTBSBXVTEAMEQO-UHFFFAOYSA-M SMILEShelp_outline CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 180 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,006 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16513 | RHEA:16514 | RHEA:16515 | RHEA:16516 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
Cloning and analysis of the L-lactate utilization genes from Streptococcus iniae.
Gibello A., Collins M.D., Dominguez L., Fernandez-Garayzabal J.F., Richardson P.T.
The presence of lactate oxidase was examined in eight Streptococcus species and some related species of bacteria. A clone (pGR002) was isolated from a genomic library of Streptococcus iniae generated in Escherichia coli, containing a DNA fragment spanning two genes designated lctO and lctP. We sho ... >> More
The presence of lactate oxidase was examined in eight Streptococcus species and some related species of bacteria. A clone (pGR002) was isolated from a genomic library of Streptococcus iniae generated in Escherichia coli, containing a DNA fragment spanning two genes designated lctO and lctP. We show that these genes are likely to be involved in the L-lactic acid aerobic metabolism of this organism. This DNA fragment has been sequenced and characterized. A comparison of the deduced amino acid sequence of LctP protein demonstrated that the protein had significant homology with the L-lactate permeases of other bacteria. The amino acid sequence of the LctO protein of S. iniae also showed a strong homology to L-lactate oxidase from Aerococcus viridans and some NAD-independent lactate dehydrogenases, all belonging to the family of flavin mononucleotide-dependent alpha-hydroxyacid-oxidizing enzymes. Biochemical assays of the gene products confirm the identity of the genes from the isolated DNA fragment and reveal a possible role for the lactate oxidase from S. iniae. This lactate oxidase is discussed in relation to the growth of the organism in response to carbon source availability. << Less
Appl. Environ. Microbiol. 65:4346-4350(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
Mechanism of action and crystallization of lactic oxidative decarboxylase from Mycobacterium phlei.
SUTTON W.B.