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PubMed2000

Tight binding of pyridoxal 5'-phosphate to recombinant Escherichia coli pyridoxine 5'-phosphate oxidase.

Escherichia coli pyridoxine (pyridoxamine) 5'-phosphate oxidase (PNPOx) catalyzes the oxidation of pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate (PLP) using flavin mononucleotide (FMN) as the immediate electron acceptor and oxygen as the ultimate electron acceptor. This reaction serves as the terminal step in the de novo biosynthesis of PLP in E. coli. Removal of FMN from the holoenzyme results in a catalytically inactive apoenzyme. PLP molecules bind tightly to both apo- and holoPNPOx with a stoichiometry of one PLP per monomer. The unique spectral property of apoPNPOx-bound PLP suggests a non-Schiff base linkage. HoloPNPOx with tightly bound PLP shows normal catalytic activity, suggesting that the tightly bound PLP is at a noncatalytic site. The tightly bound PLP is readily transferred to aposerine hydroxymethyltransferase in dilute phosphate buffer. However, when the PNPOx. PLP complex was added to aposerine hydroxymethyltransferase suspended in an E. coli extract the rate of reactivation of the apoenzyme was several-fold faster than when free PLP was added. This suggests that PNPOx somehow targets PLP to aposerine hydroxymethyltransferase in vivo.

Apoenzymes↗
PubMed1985

Pyridoxal phosphate-unrelated inhibition of hippocampal glutamic acid decarboxylase by convulsant pyridoxal sulphate.

Previous studies from this laboratory have shown that pyridoxal-5'-sulphate, the synthetic analogue of pyridoxal phosphate, causes epileptic seizures including tonic-clonic convulsions. These seizure activities are prevented or reversed by GABA or muscimol. In an attempt to delineate the biochemical basis of these seizure processes further, we have studied and shown that pyridoxal sulphate is a competitive inhibitor of glutamic acid decarboxylase. In addition, the chronic administration of pyridoxal sulphate was shown to reduce the concentration of pyridoxal phosphate in the cerebellum, the cerebrum, and basal ganglion, but not in the hippocampus. The activity of hippocampal glutamic acid decarboxylase was reduced after 1, 3, and 5 days of chronic application of pyridoxal sulphate. The inhibition was demonstrated, whether glutamic acid decarboxylase was assayed in the presence or absence of its coenzyme pyridoxal phosphate. Unlike findings in the hippocampus, the activity of glutamic acid decarboxylase in other brain regions was unaffected following chronic application of pyridoxal sulphate. The selective toxic effects of pyridoxal sulfate to the hippocampus, a brain area well known for its high susceptibility to seizure discharges, deserve additional indepth investigation.

Animals↗
PubMed1976

Observations on the pyridoxal 5'-phosphate inhibition of DNA polymerases.

Pyridoxal 5'-phosphate at concentrations greater than 0.5 mM inhibits polymerization of deoxynucleoside triphosphate catalyzed by a variety of DNA polymerases. The requirement for a phosphate as well as aldehyde moiety of pyridoxal phosphate for inhibition to occur is clearly shown by the fact that neither pyridoxal nor pyridoxamine phosphate are effective inhibitors. Since the addition of nonenzyme protein or increasing the amount of template primer exerted no protective effect, there appears to be specific affinity between pyridoxal phosphate and polymerase protein. The deoxynucleoside triphosphates, however, could reverse the inhibition. The binding of pyridoxal 5'-phosphate to enzyme appears to be mediated through classical Schiff base formation between the pyridoxal phosphate and the free amino group(s) present at the active site of the polymerase protein. Kinetic studies indicate that inhibition by pyridoxal phosphate is competitive with respect to substrate deoxynucleoside triphosphate(s).

Animals↗
PubMed1994

The utilization of intravenously infused pyridoxine in humans.

The utilization of a usual dose of intravenously infused pyridoxine (100 mg pyridoxine hydrochloride) was investigated in ten healthy males. Blood plasma and erythrocytes were investigated by means of high-performance liquid chromatography. Detectable metabolites in blood plasma were pyridoxine, pyridoxal 5'-phosphate, pyridoxal and 4-pyridoxic acid. In erythrocytes pyridoxine, pyridoxal 5'-phosphate, pyridoxal, and pyridoxamine 5'-phosphate were found. From their concentration-time curves rate constants of elimination and invasion, volume of distribution (pyridoxine) and the areas under the curves were calculated. Values for concmax and tmax are reported. A comparison with earlier results of oral pyridoxine administration revealed a better utilization after intravenous than after oral application, i.e. a greater build-up of coenzyme forms. A regulatory phenomenon in erythrocytes caused by high doses of pyridoxine is described. In view of the potential toxicity of pyridoxine the doses used in parenteral nutrition are called into question.

Adult↗
PubMed1984

Relationship between pyridoxal 5'-phosphate deficiency and aminotransferase levels in alcoholic hepatitis.

The relationship between pyridoxal phosphate deficiency and activities of serum and liver aminotransferases was studied in 12 patients with alcoholic hepatitis. Plasma pyridoxal phosphate and the activities of liver aminotransferases were initially decreased in the patients, as compared with mean values in controls with normal hepatic histology. Addition of pyridoxal phosphate to liver homogenates increased liver alanine aminotransferase, but not aspartate aminotransferase, in all patients with initially low plasma pyridoxal phosphate. After 1 mo of abstinence from alcohol, with intake of an adequate diet and pyridoxine supplementation, plasma pyridoxal phosphate increased in all patients with initially low values (p less than 0.02). Serum aspartate aminotransferase decreased, whereas serum alanine aminotransferase increased, resulting in a decrease in their ratio in serum (p less than 0.001). Liver alanine aminotransferase increased (p less than 0.005), whereas liver aspartate aminotransferase remained unchanged. These data suggest that pyridoxal 5'-phosphate depletion is partially responsible for the low serum alanine to aspartate aminotransferase ratio that is typical of patients with alcoholic hepatitis.

Acute Disease↗
PubMed1975

Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine.

Pig plasma benzylamine oxidase is a protein containing cupric copper and pyridoxal phosphate. The pyridoxal phosphate is stably linked to the enzyme. Discrepancies in the numbers of active sites per molecule of enzyme are reported in the literature. This paper shows that the fully active pure enzyme contains 3 mol of pyridoxal phosphate per mol, whereas enzymes with a lower specific activity are shown by titration with phenylhydrazine to have a lower pyrdoxal phosphate content.

Animals↗
PubMed1991

Spectroscopic study of the Schiff bases of dodecylamine with pyridoxal 5'-phosphate and 5'-deoxypyridoxal. A model for the Schiff bases of pyridoxal 5'-phosphate in biological systems.

We recorded the absorption spectra of the Schiff bases of pyridoxal 5'-phosphate (PLP) and 5'-deoxypyridoxal (DPL) with dodecylamine (DOD) at different pH values. By applying deconvolution techniques to the spectra and analysing their different components we found that the above-mentioned Schiff bases in aqueous solutions of pH 7 adopted a conformation in which the pyridine ring is embedded in a very hydrophobic medium from which water is virtually completely excluded. This conformation in the same as that adopted by PLP when it acts as coenzyme for some enzymes such as glycogen phosphorylase. The experimental results obtained also show such a conformation to be highly favoured but sensitive to the protonation of the pyridine nitrogen, which makes the aromatic ring more readily accessible to the solvent.

Amines↗
PubMed1999

Inactivation of the reconstituted oxoglutarate carrier from bovine heart mitochondria by pyridoxal 5'-phosphate.

The effect of pyridoxal 5'-phosphate and some other lysine reagents on the purified, reconstituted mitochondrial oxoglutarate transport protein has been investigated. The inhibition of oxoglutarate/oxoglutarate exchange by pyridoxal 5'-phosphate can be reversed by passing the proteoliposomes through a Sephadex column but the reduction of the Schiff's base by sodium borohydride yielded an irreversible inactivation of the oxoglutarate carrier protein. Pyridoxal 5'-phosphate, which caused a time- and concentration-dependent inactivation of oxoglutarate transport with an IC50 of 0.5 mM, competed with the substrate for binding to the oxoglutarate carrier (Ki = 0.4 mM). Kinetic analysis of oxoglutarate transport inhibition by pyridoxal 5'-phosphate indicated that modification of a single amino acid residue/carrier molecule was sufficient for complete inhibition of oxoglutarate transport. After reduction with sodium borohydride [3H]pyridoxal 5'-phosphate bound covalently to the oxoglutarate carrier. Incubation of the proteoliposomes with oxoglutarate or L-malate protected the carrier against inactivation and no radioactivity was found associated with the carrier protein. In contrast, glutarate and substrates of other mitochondrial carrier proteins were unable to protect the carrier. Mersalyl, which is a known sulfhydryl reagent, also failed to protect the oxoglutarate carrier against inhibition by pyridoxal 5'-phosphate. These results indicate that pyridoxal 5'-phosphate interacts with the oxoglutarate carrier at a site(s) (i.e., a lysine residue(s) and/or the amino-terminal glycine residue) which is essential for substrate translocation and may be localized at or near the substrate-binding site.

Animals↗
PubMed1990

In vitro evidence for a relationship between magnesium and vitamin B-6.

Vitamin B-6 and magnesium appear to interact in vivo and it has been suggested that vitamin B-6 may enhance transport or accumulation of magnesium in cells. The purpose of this study was to evaluate the possibility of the formation of B-6 vitamer-Mg complexes in vitro using spectrophotometric analysis of ultraviolet or visible spectra or change in fluorescence intensity of B-6 vitamers. Pyridoxal phosphate but not pyridoxal appears to form a complex with Mg as evidenced by a change in the ultraviolet and visible spectra with an increase in absorption and spectral shift in the visible maxima from 389 to 388 nm and a decrease in the ultraviolet absorption maxima at 296 nm. Addition of Mg to pyridoxal phosphate but not the other B-6 vitamers enhanced the fluorescent intensity of pyridoxal phosphate at least threefold and evoked a spectral shift in both the fluorescence excitation and emission maximum. Electrochemical titration of pyridoxal phosphate in the presence of Mg affects the pKa- of the phenolic hydroxyl and the secondary phosphate ionization. These data collectively indicate that pyridoxal phosphate, but not pyridoxal, appears to form a coordinated complex with Mg and the coordination site is likely to be related to the primary phosphate and aldehyde moiety of pyridoxal phosphate.

Chelating Agents↗