Results 21 to 30 of about 38,650 (260)

Identification of the pyridoxal 5'-phosphate allosteric site in human pyridox(am)ine 5'-phosphate oxidase. [PDF]

open access: yesProtein Sci
AbstractAdequate levels of pyridoxal 5′‐phosphate (PLP), the catalytically active form of vitamin B6, and its proper distribution in the body are essential for human health. The PLP recycling pathway plays a crucial role in these processes and its defects cause severe neurological diseases.
Barile A   +11 more
europepmc   +3 more sources

Pyridoxal 5'-phosphate is a slow tight binding inhibitor of E. coli pyridoxal kinase. [PDF]

open access: yesPLoS ONE, 2012
Pyridoxal 5'-phosphate (PLP) is a cofactor for dozens of B(6) requiring enzymes. PLP reacts with apo-B(6) enzymes by forming an aldimine linkage with the ε-amino group of an active site lysine residue, thus yielding the catalytically active holo-B(6 ...
Mohini S Ghatge   +10 more
doaj   +1 more source

Vitamin B6 Acquisition and Metabolism in Schistosoma mansoni

open access: yesFrontiers in Immunology, 2021
Schistosomes are parasitic platyhelminths that currently infect >200 million people globally. The adult worms can live within the vasculature of their hosts for many years where they acquire all nutrients necessary for their survival and growth.
Akram A. Da’dara   +4 more
doaj   +1 more source

Pyridoxal in the Cerebrospinal Fluid May Be a Better Indicator of Vitamin B6–dependent Epilepsy Than Pyridoxal 5′-Phosphate [PDF]

open access: yes, 2020
Background We aimed to demonstrate the biochemical characteristics of vitamin B6–dependent epilepsy, with a particular focus on pyridoxal 5′-phosphate and pyridoxal in the cerebrospinal fluid. Methods Using our laboratory database, we identified patients
Akiyama, Tomoyuki   +19 more
core   +1 more source

NRF2 signalling in cytoprotection and metabolism

open access: yesBritish Journal of Pharmacology, EarlyView., 2023
The KEAP1‐NRF2 system plays a central role in cytoprotection in defence mechanisms against oxidative stress. The KEAP1‐NRF2 system has been regarded as a sulfur‐utilizing cytoprotective mechanism, because KEAP1 serves as a biosensor for electrophiles by using its reactive thiols and NRF2 is a transcriptional factor regulating genes involved in sulfur ...
Shohei Murakami   +4 more
wiley   +1 more source

Pyridoxal 5′-Phosphate-dependent Catalytic Antibody [PDF]

open access: hybridJournal of Biological Chemistry, 1996
Cofactors might efficiently extend the catalytic potential of antibodies. Monoclonal antibodies against Nalpha-phosphopyridoxyl-L-lysine were screened for: 1) binding of 5'-phosphopyridoxyl amino acids, 2) binding of Schiff base of pyridoxal 5'-phosphate (PLP) and amino acids, the first intermediate of all PLP-dependent reactions, and 3) catalysis of ...
Svetlana Gramatikova, Philipp Christen
openalex   +4 more sources

SNZ3 Encodes a PLP Synthase Involved in Thiamine Synthesis in Saccharomyces cerevisiae

open access: yesG3: Genes, Genomes, Genetics, 2019
Pyridoxal 5′-phosphate (the active form of vitamin B6) is a cofactor that is important for a broad number of biochemical reactions and is essential for all forms of life.
Michael D. Paxhia, Diana M. Downs
doaj   +1 more source

Circulating pyridoxal 5′-phosphate in serum and whole blood: implications for assessment of vitamin B6 status

open access: yesJournal of Laboratory Medicine, 2023
Concentrations of pyridoxal 5′-phosphate (PLP) in serum and whole blood are routinely measured. The suitability of these markers in capturing vitamin B6 insufficiency is not well studied.
Obeid Rima   +2 more
doaj   +1 more source

Competition of Pyridoxal 5'-Phosphate with Ribulose 1,5-Bisphosphate and Effector Sugar Phosphates at the Reaction Centers of the Spinach Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase [PDF]

open access: yes, 1980
The Stimulation of the carboxylase reaction by effectors of ribulose 1,5-bisphosphate carboxyl­ ase/oxygenase displays higher sensitivity towards pyridoxal 5'-phosphate inhibition than the catalytical process itself. Pyridoxal 5'-phosphate binding to the
Gaudszun, Thomas   +3 more
core   +1 more source

Binding of Pyridoxal 5-Phosphate to Cystathionase

open access: hybridJournal of Biological Chemistry, 1973
Abstract The binding of pyridoxal 5-phosphate to the apoprotein of the enzyme cystathionase from rat liver was investigated by two independent methods, absorption and fluorescence spectroscopy. The increase in absorbance at 525 nm associated with Schiff's base formation was used to investigate the binding of pyridoxal-5-P at a protein concentration of ...
Kyung-Ja Oh, Jorge E. Churchich
openalex   +3 more sources

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