Results 231 to 240 of about 150,374 (260)
Some of the next articles are maybe not open access.

Regulation of pyridoxal 5′-phosphate metabolism in liver

Biochemical and Biophysical Research Communications, 1974
Abstract The pyridoxal 5′-phosphate content of liver in vivo and of hepatocytes in vitro remains unaltered in the presence of excess unphosphorylated vitamin B6 precursors. Studies with isolated hepatocytes and subcellular fractions show that while product inhibition of pyridoxine phosphate oxidase does not limit synthesis sufficiently to
Robert L. Veitch   +2 more
openaire   +3 more sources

Antibodies against pyridoxal 5′-phosphate and pyridoxamine 5′-phosphate

Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract 1. 1. The antigenicity of pyridoxal 5′-phosphate in rabbits was tested by immunization of the animals with the coenzyme coupled to bovine serum albumin. The coupling of pyridoxal phosphate to albumin, as well as to other proteins, was achieved by reduction (at pH 7·5) with sodium borohydride. 2. 2.
Concepción González   +2 more
openaire   +2 more sources

Mechanism of formation of the internal aldimine in pyridoxal 5'-phosphate-dependent enzymes.

Journal of the American Chemical Society, 2011
In this paper we studied the mechanism of formation of the internal aldimine, a common intermediate to most pyridoxal 5'-phosphate (PLP)-dependent enzymes.
Eduardo F T Oliveira   +3 more
semanticscholar   +1 more source

Reactivity of pyridoxal 5-phosphate residues of cystathionase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 1. 1.|The pyridoxal-5-P residues of the enzyme cystathionase from rat liver show different reactivity towards chemical reagents such as cycloserine and sodium borohydride. Although the enzyme contains three molecules of pyridoxal-5-P per 150 000 molecular weight, only one of the pyridoxal-5-P chromophores reacts with cycloserine at pH ...
Jorge E. Churchich, Julie Bieler
openaire   +3 more sources

Computational Mechanistic Studies Addressed to the Transimination Reaction Present in All Pyridoxal 5'-Phosphate-Requiring Enzymes.

Journal of Chemical Theory and Computation, 2011
The pyridoxal-5'-phosphate-dependent enzymes (PLP enzymes) catalyze a myriad of biochemical reactions, being actively involved in the biosynthesis of amino acids and amino acid-derived metabolites as well as in the biosynthetic pathways of amino sugars ...
N. M. Cerqueira   +2 more
semanticscholar   +1 more source

A novel coenzymatic function of pyridoxal 5′‐phosphate

BioEssays, 1986
AbstractPyridoxal 5′‐phosphate, the vitamin B6 derivative, acts as the coenzyme of many enzymes involved in amino acid metabolism. Exceptionally, this compound was found covalently bound to glycogen phosphorylase, the key enzyme in the regulation of glycogen metabolism.
Mitsuo Tagaya, Toshio Fukui
openaire   +3 more sources

Pyridoxal 5-Phosphate and Calcium Channels

2000
The BAY K 8644 -induced influx of 45Calcium into intracellular compartment of artery segments of normal rats was blocked by pyridoxal phosphate (PLP) as well as by the dihydropyridine-sensitive calcium channel antagonists (CCA). PLP also decreased bindingin vitroof CCA to membrane preparations from normal vascular tissue.
Krishnamurti Dakshinamurti   +4 more
openaire   +2 more sources

Pyridoxal 5′-Phosphate (PLP)

Nutrition Reviews, 2009
William J. Stone   +3 more
openaire   +2 more sources

Pyridoxal 5'-phosphate and related metabolites in hypophosphatasia: Effects of enzyme replacement therapy.

Molecular Genetics and Metabolism, 2018
T. Akiyama   +18 more
semanticscholar   +1 more source

Home - About - Disclaimer - Privacy