Induction of Plant Pyridoxine (Pyridoxamine) 5′-Phosphate Oxidase Activity by Light
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چکیده
منابع مشابه
Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12.
We report the purification and enzymological characterization of Escherichia coli K-12 pyridoxine (pyridoxamine) 5'-phosphate (PNP/PMP) oxidase, which is a key committed enzyme in the biosynthesis of the essential coenzyme pyridoxal 5'-phosphate (PLP). The enzyme encoded by pdxH was overexpressed and purified to electrophoretic homogeneity by four steps of column chromatography. The purified Pd...
متن کاملBrain pyridoxine-5-phosphate oxidase. Modulation of its catalytic activity by reaction with pyridoxal 5-phosphate and analogs.
Pyridoxine-5-P oxidase, the flavoprotein involved in the oxidation of pyridoxamine-5-P and pyridoxine-5-P to pyridoxal-5-P, has been isolated and purified to homogeneity using sheep brain tissues. Inactivation of the oxidase by bis-pyridoxal-5-P results in binding of the inhibitor to specific lysyl residues. After NaBH4 reduction of the inactivated enzyme, it was found that 1 P-pyridoxyl-pyrido...
متن کاملMolecular basis of reduced pyridoxine 5'-phosphate oxidase catalytic activity in neonatal epileptic encephalopathy disorder.
Mutations in pyridoxine 5'-phosphate oxidase are known to cause neonatal epileptic encephalopathy. This disorder has no cure or effective treatment and is often fatal. Pyridoxine 5'-phosphate oxidase catalyzes the oxidation of pyridoxine 5'-phosphate to pyridoxal 5'-phosphate, the active cofactor form of vitamin B(6) required by more than 140 different catalytic activities, including enzymes in...
متن کاملPyridoxamine-5'-phosphate oxidase exhibits no specificity in prochiral hydrogen abstraction from substrate.
The stereochemistry for hydrogen removal from pyridoxamine 5'-phosphate with liver pyridoxine (pyridoxamine)-5'-phosphate oxidase was examined to determine whether or not there are significant steric constraints at the substrate region of the active site of the oxidase. For this, pyridoxal 5'-phosphate was reduced with tritium-labeled sodium borohydride in ammoniacal solution to yield racemical...
متن کاملErythrocyte pyridoxamine phosphate oxidase activity: a potential biomarker of riboflavin status?
BACKGROUND Riboflavin status is commonly measured by the in vitro stimulation of erythrocyte glutathione reductase with flavin adenine dinucleotide and expressed as an erythrocyte glutathione reductase activation coefficient (EGRAC). However, this assay is insensitive to poor riboflavin status in subjects with glucose-6-phosphate dehydrogenase (G6PD) deficiency. Because G6PD deficiency is commo...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1981
ISSN: 0002-1369
DOI: 10.1080/00021369.1981.10864776