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Activation of pyridoxal kinase by metallothionein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
Brain pyridoxal kinase, which uses ATP complexed to either Zn(II) or Co(II) as substrates, displays high catalytic activity in the presence of Zn-thionein and Co-thionein. Several steps intervene in the process of pyridoxal kinase activation, i.e., binding of Zn ions to ATP and interaction between Zn-ATP and the enzyme. Equilibrium binding studies show
J E, Churchich, G, Scholz, F, Kwok
openaire   +2 more sources

Inhibition of Pyridoxal Kinase by Methylxanthines

Enzyme, 1990
In the presence of saturating concentrations of adenosine triphosphate (ATP) and rate-limiting amounts of pyridoxal, theophylline was found to inhibit sheep brain pyridoxal kinase (EC 2.7.1.35) competitively. The apparent inhibition constant (Ki) of theophylline for pyridoxal kinase was determined as 8.7 mumol/l. Theophylline concentrations of up to 60
J B, Ubbink   +3 more
openaire   +2 more sources

Binding of a photoaffinity analogue of pyridoxal to pyridoxal kinase

European Journal of Biochemistry, 1990
The binding of pyridoxal analogues to the structural domains of pyridoxal kinase was studied by fluorescence spectroscopy and chromatographic techniques. Two fragments of 24 and 16 kDa, arising from limited proteolysis of the native enzyme, were separated by ion‐exchange chromatography and used for binding studies with pyridoxal oxime.
G, Scholz, F, Kwok, J E, Churchich
openaire   +2 more sources

Pyridoxal Kinase from Leishmania donovani in complex with ADP and Pyridoxamine

, 2020
The enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal-5′-phosphate (PLP) using ATP as the co-factor. The product pyridoxal-5′-phosphate plays a key role in several biological processes such as transamination ...
S. Are   +3 more
semanticscholar   +1 more source

On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5′-phosphate

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015
Pyridoxal 5'-phosphate (PLP), the catalytically active form of vitamin B6, plays a crucial role in several cellular processes. In most organisms, PLP is recycled from nutrients and degraded B6-enzymes in a salvage pathway that involves pyridoxal kinase (PLK), pyridoxine phosphate oxidase and phosphatase activities.
DI SALVO, Martino Luigi   +6 more
openaire   +2 more sources

Exploring the role of pyridoxal kinase: a key player in vitamin B6 metabolism

Endocrinology & Metabolism International Journal
Cancer remains one of the most challenging diseases to treat, demanding innovative approaches to combat its complexity and heterogeneity. In recent years, Pyridoxal kinase (PDXK), a critical enzyme in the vitamin B6 metabolic pathway, has emerged as a ...
Pallabi Banerjee   +6 more
semanticscholar   +1 more source

Biotransformation of pyridoxal 5'-phosphate from pyridoxal by pyridoxal kinase (pdxY) to support cadaverine production in Escherichia coli.

Enzyme and Microbial Technology, 2017
Cadaverine, a five-carbon diamine (1,5-diaminopentane), can be made by fermentation or direct bioconversion and plays an important role as a building block of polyamides. Lysine decarboxylase (CadA) transforms L-lysine to cadaverine and pyridoxal 5'-phosphate (PLP) can increases conversion rate and yield as a cofactor.
Jung Ho Kim   +9 more
semanticscholar   +3 more sources

Pyridoxal kinase, encoded by the PDXK gene, is differentially expressed in the brains of patients with schizophrenia.

, 2020
Visual and auditory hallucinations are a cardinal feature of psychotic disorders (1). We mined published and public microarray datasets (2, 3) to discover differentially expressed genes in schizophrenia and schizoaffective disorder.
Shahan Mamoor
semanticscholar   +1 more source

Cloning and characterization of Arabidopsis thaliana pyridoxal kinase

Planta, 2002
Pyridoxal kinase (PK; EC 2.7.1.35), a key enzyme in vitamin B(6) metabolism, was cloned from Arabidopsis thaliana (L.) Heynh. and characterized. The amino acid sequence of the A. thaliana PK was found to be similar to the mammalian enzyme, with a homology of more than 40%. Characterization studies showed that the kinase is a dimeric molecule consisting
Hon-Kei, Lum   +2 more
openaire   +2 more sources

A rapid fluorometric assay for erythrocyte pyridoxal kinase

Biochemical Medicine, 1982
Abstract We describe a method for measurement of erythrocyte pyridoxal kinase activity in hemolysates, in which pyridoxal phosphate is oxidized and assayed by fluorometry. We also use this method to measure pyridoxal phosphate synthesis by intact erythrocytes suspended with pyridoxal or pyridoxine.
J A, Kark   +4 more
openaire   +2 more sources

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