
Biochemistry, Lactate Dehydrogenase - StatPearls - NCBI Bookshelf
2023年5月1日 · LDH is a cytoplasmic enzyme that is present in almost all tissues but at high concentrations in muscle, liver, and kidney. Red blood cells also contain moderate concentrations of this enzyme. LDH exhibits five isomeric forms assembled in tetramers of either of the two types of subunits, namely muscle (M) and heart (H).
Discovery of a novel lactate dehydrogenase tetramerization …
We report the identification and characterization of a new cluster of interactions in the LDH tetrameric interface. Using nanoscale differential scanning fluorimetry, chemical denaturation, and mass photometry, we identified several residues (E62, D65, L71, and F72) essential for LDH tetrameric stability.
Novel Peptide Inhibitors for Lactate Dehydrogenase A (LDHA): A …
In this study, we employed in silico methods to design inhibitory peptides for lactate dehydrogenase through the disturbance in tetramerization of the enzyme.
Lactate dehydrogenase - Wikipedia
Enzymatically active lactate dehydrogenase is consisting of four subunits (tetramer). The two most common subunits are the LDH-M and LDH-H peptides, named for their discovery in muscle and heart tissue, and encoded by the LDHA and LDHB genes, respectively.
Substrate Channeling via a Transient Protein-Protein Complex: The …
2020年6月26日 · Here we have provided a new set of evidence that shows that LDH and GAPDH tetramers can form a transient supramolecular complex that can simultaneously support channeled and diffusive reactions.
The two LDH homotetramers, lactate dehydro-genase heart isozyme homotetramer (LDH-1) (LDH-H4) and lactate dehydrogenase muscle isozyme homotetramer (LDH-5) (LDH-M4), are the most extensively studied forms of LDH and constitute appealing targets …
The tetramerisation of ldh subunits in human serum
1976年1月1日 · Firstly, the random nature of the process suggests that the binding sites of the different human LDH subunits must be very similar, since no preferential binding is observed. Secondly, the LDH tetramers must exist in a state of dynamic equilibrium in serum solution, with free monomer, dimer and trimer. This is inferred from the Fig. 5.
(PDF) Discovery of a novel lactate dehydrogenase ... - ResearchGate
2021年2月1日 · We report the identification and characterization of a new cluster of interactions in the LDH tetrameric interface. Using nanoscale differential scanning fluorimetry, chemical denaturation and...
LDH tetramers and isotype distribution in the human body.
The authors further describe the 5 main subunits of LDH enzyme existing in human tissue, comprising of different variants of the 2 tetramere subunits with LDH-5 being the most prevalent isotype...
Discovery of a novel lactate dehydrogenase tetramerization domain using ...
We report the identification and characterization of a new cluster of interactions in the LDH tetrameric interface. Using nanoscale differential scanning fluorimetry, chemical denaturation, and mass photometry, we identified several residues (E62, D65, L71, and F72) essential for LDH tetrameric stability.