l-Lactate treatment by photosynthetic cyanobacteria expressing heterogeneous l-lactate dehydrogenase [PDF]
Scientific Reports, 2023 l-Lactate is a major waste compound in cultured animal cells. To develop a sustainable animal cell culture system, we aimed to study the consumption of l-lactate using a photosynthetic microorganism.
Yuichi Kato +5 more
doaj +5 more sources
The mitochondrial L-lactate dehydrogenase affair [PDF]
Frontiers in Neuroscience, 2014 The existence of a mitochondrial L-lactate dehydrogenase (m-L-LDH) suggested by Dianzani (1951), was shown by Baba and Sharma (1971) with the enzyme located in the mitochondrial matrix; later Brooks et al. (1999) proposed the intracellular lactate shuttle and in the third millennium the existence of m-L-LDH was definitively been confirmed in mammalian,
SALVATORE ePASSARELLA +2 more
doaj +6 more sources
NAD-Independent l-Lactate Dehydrogenase Required for l-Lactate Utilization in Pseudomonas stutzeri A1501 [PDF]
Journal of Bacteriology, 2015 ABSTRACTNAD-independentl-lactate dehydrogenases (l-iLDHs) play important roles inl-lactate utilization of different organisms. All of the previously reportedl-iLDHs were flavoproteins that catalyze the oxidation ofl-lactate by the flavin mononucleotide (FMN)-dependent mechanism.
Min Lv +6 more
semanticscholar +5 more sources
Characterization of the L-lactate dehydrogenase from Aggregatibacter actinomycetemcomitans. [PDF]
PLoS ONE, 2009 Aggregatibacter actinomycetemcomitans is a Gram-negative opportunistic pathogen and the proposed causative agent of localized aggressive periodontitis. A.
Stacie A Brown, Marvin Whiteley
doaj +7 more sources
The Core of Allosteric Motion in Thermus caldophilus l-Lactate Dehydrogenase [PDF]
Journal of Biological Chemistry, 2014 For Thermus caldophilus L-lactate dehydrogenase (TcLDH), fructose 1,6-bisphosphate (FBP) reduced the pyruvate S(0.5) value 10(3)-fold and increased the V(max) value 4-fold at 30 °C and pH 7.0, indicating that TcLDH has a much more T state-sided allosteric equilibrium than Thermus thermophilus L-lactate dehydrogenase, which has only two amino acid ...
Yoko Ikehara +8 more
semanticscholar +5 more sources
Substrate Channeling via a Transient Protein-Protein Complex: The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase [PDF]
Sci Rep, 2020 Substrate channeling studies have frequently failed to provide conclusive results due to poor understanding of this subtle phenomenon. We analyzed the mechanism of NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate ...
Ž. Svedružić +3 more
semanticscholar +2 more sources
NAD-independent L-lactate dehydrogenase is required for L-lactate utilization in Pseudomonas stutzeri SDM. [PDF]
PLoS ONE, 2012 BACKGROUND: Various Pseudomonas strains can use L-lactate as their sole carbon source for growth. However, the L-lactate-utilizing enzymes in Pseudomonas have never been identified and further studied. METHODOLOGY/PRINCIPAL FINDINGS: An NAD-independent L-
Chao Gao +6 more
doaj +5 more sources
Lactic dehydrogenase enzyme and L-lactate in preeclampsia. A review [PDF]
, 2023 Background Preeclampsia is the most important hypertensive disease complicating human pregnancy in the world. It is a condition of placental origin with adverse effects on the placenta itself, the fetus and the mother. Its pathophysiology is complex and incompletely known.
Juan Gustavo Vázquez Rodríguez
openalex +3 more sources
Enantioselective Biosynthesis of L-Phenyllactic Acid From Phenylpyruvic Acid In Vitro by L-Lactate Dehydrogenase Coupling With Glucose Dehydrogenase [PDF]
Frontiers in Bioengineering and Biotechnology, 2022 As a valuable versatile building block, L-phenyllactic acid (L-PLA) has numerous applications in the fields of agriculture, pharmaceuticals, and biodegradable plastics. However, both normally chemically synthesized and naturally occurring PLA are racemic,
Dong Zhang +5 more
doaj +2 more sources
D- and L-lactate dehydrogenases during invertebrate evolution [PDF]
BMC Evolutionary Biology, 2008 The L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate, belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes.
Melania E. Cristescu +3 more
openalex +6 more sources