Results 61 to 69 of about 69 (69)
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Mechanisms of the inhibition of human erythrocyte pyridoxal kinase by drugs

Biochemical Pharmacology, 1997
The aim of this study was to investigate the interaction between drugs chosen for their clinical neurotoxicity or chemical structure and vitamin B6 metabolism. After a preliminary screening of drugs to determine their potential inhibitory effect on erythrocyte nonpurified pyridoxal kinase (PLK) (EC 2.7.1.35), additional investigations, including ...
Pascale Lainé-Cessac   +2 more
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[109] Pyridoxal kinase from brewer's yeast

1955
Publisher Summary This chapter discusses the determination of pyridoxal kinase from Brewer's yeast. Pyridoxal phosphate, formed by kinase action, is measured by the activation of a crude tyrosine apodecarboxylase preparation from Streptococcus faecalis . The assay is proportional to pyridoxal phosphate over the range of 1 to 10 mμM. (1 to 10 units).
I.C. Gunsalus, W.E. Razzell
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The interaction of paramagnetic ions chelated to ATP with pyridoxal analogues

European Journal of Biochemistry, 1991
Fluorescence spectroscopy, static and dynamic, was applied to deduce proximity relationships between paramagnetic metal ions chelated to ATP and the inhibitor pyridoxal oxime bound to the site of the substrate pyridoxal. The fluorescence yield of free pyridoxal oxime is considerably reduced in the presence of CoCl2 (1 mM) due to the formation of a non ...
Jorge E. Churchich, Francis Kwok
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Structure-Function Relationships of Porcine Pyridoxal Kinase

2000
Pyridoxal kinase (PK) catalyzes the formation of pyridoxal-5-phosphate (PLP) from pyridoxal (PL), ATP and a divalent cation (Zn2+). So far, there is no three-dimensional structure of PK available. Site-directed mutagenesis was carried out to study the importance of three conserved residues: Tyr137, Gly242 and G1y244. The mutants (Y137F, G242A and G244A)
H. Y. Wong   +4 more
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Inactivation of microbial pyridoxal kinase by pyridoxal.

Acta vitaminologica et enzymologica, 1982
Pyridoxal kinase from Escherichia coli and bakers' yeast was inactivated by pyridoxal while the enzyme from rat and pig brain was not. The inactivation of the enzyme purified from E. coli was reversible and was rendered irreversible by the reduction with NaBH4.
Y, Furukawa, R, Yamada, A, Iwashima
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Subcellular distribution of pyridoxal kinase in ox retina.

The Italian journal of biochemistry, 1976
PL kinase activity has been determined in primary and secondary subcellular fractions of ox retina. Enzymic activity is predominantly located in the soluble fraction (S3). About 65% of the recovered PL kinase activity of crude mitochondria is released from synaptosomal fraction after hypoosmotic treatment. PL kinase activity in supernatant fraction (S3)
MACAIONE, Salvatore   +2 more
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Pyridoxal Kinase: Inhibitors Bound to the Pyridoxal Binding Site

1991
GLEN SCHOLZ   +2 more
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Pyridoxal kinase

1997
Dietmar Schomburg, Dörte Stephan
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