P00344 · LDH_GEOSE

Function

function

Catalyzes the conversion of lactate to pyruvate.

Catalytic activity

Activity regulation

Allosterically activated by fructose 1,6-bisphosphate (FBP). The improvement in affinity for substrate occurs in two steps; the binding of fructose 1,6-bisphosphate (FBP) to the dimer, and the dimer to tetramer conversion.

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.

Features

Showing features for binding site, active site.

131720406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site16-17NAD+ (UniProtKB | ChEBI)
Binding site38NAD+ (UniProtKB | ChEBI)
Binding site43NAD+ (UniProtKB | ChEBI)
Binding site69NAD+ (UniProtKB | ChEBI)
Binding site83-84NAD+ (UniProtKB | ChEBI)
Binding site86substrate
Binding site92substrate
Binding site105NAD+ (UniProtKB | ChEBI)
Binding site122-124NAD+ (UniProtKB | ChEBI)
Binding site124-127substrate
Binding site147NAD+ (UniProtKB | ChEBI)
Binding site152-155substrate
Binding site157beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator
Binding site169-172beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric activator
Active site179Proton acceptor
Binding site233substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionL-lactate dehydrogenase activity
Molecular FunctionNAD binding
Biological Processglycolytic process
Biological Processlactate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-lactate dehydrogenase
  • EC number
  • Short names
    L-LDH

Gene names

    • Name
      ldh
    • Synonyms
      lct

Organism names

Accessions

  • Primary accession
    P00344

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis157This mutant undergoes a reversible subunit assembly from dimer to tetramer. However, the tetramer mutant is much more stable than the wild type, and is destabilized rather than stabilized by binding the allosteric regulator, fructose 1,6-bisphosphate (FBP). The mutation weakens the binding of fructose 1,6-bisphosphate (FBP) to both the dimeric and tetrameric forms, and almost abolishes any stimulatory effect.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001683281-317L-lactate dehydrogenase
Modified residue224Phosphotyrosine

Keywords

Interaction

Subunit

Exists as a dimer and a tetramer (dimer of dimers). The conversion occurs via the binding of fructose 1,6-bisphosphate (FBP) to the dimer.

Family & Domains

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    317
  • Mass (Da)
    34,863
  • Last updated
    1988-01-01 v1
  • Checksum
    4B146CF681C91046
MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKLVESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFTR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict113in Ref. 2; AAA22567

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M14788
EMBL· GenBank· DDBJ
AAA22568.1
EMBL· GenBank· DDBJ
Genomic DNA
M19396
EMBL· GenBank· DDBJ
AAA22567.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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