Chemoenzymatic synthesis of 1-deaza-pyridoxal 5′-phosphate

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Chemoenzymatic synthesis of 1-deaza-pyridoxal 5'-phosphate.

The first synthesis of 1-deaza-pyridoxal 5'-phosphate (2-formyl-3-hydroxy-4-methylbenzyl phosphate) is described. The chemoenzymatic approach described here is a reliable route to this important isosteric pyridoxal phosphate analogue. This work enables elucidation of the role of the pyridine nitrogen in pyridoxal 5'-phosphate dependent enzymes.

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Binding of Pyridoxal 5'-Phosphate

1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo(a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the...

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Transfer of pyridoxal 5'-phosphate from albumin-pyridoxal 5'-phosphate complex to apo-aspartate aminotransferase.

Pyridoxal 5•L-phosphate (PLP) is known to combine with bovine serum albumin to form a(1:1) complex which scarcely dissociates, even when subjected to intensive dialysis. When this complex was incubated with apo-aspartate aminotransferase (apoGOT) for an appropriate time and the preincubated mixture then submitted to the usual GOT assay, the appearance of GOT activity was obviously confirmed, in...

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Biomedical aspects of pyridoxal 5'-phosphate availability.

The biologically active form of vitamin B6, pyridoxal 5'-phosphate (PLP), is a cofactor in over 160 enzyme activities involved in a number of metabolic pathways, including neurotransmitter synthesis and degradation. In humans, PLP is recycled from food and from degraded PLP-dependent enzymes in a salvage pathway requiring the action of pyridoxal kinase, pyridoxine 5'-phosphate oxidase and phosp...

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Binding of pyridoxal 5-phosphate to cystathionase.

The binding of pyridoxal 5-phosphate to the apoprotein of the enzyme cystathionase from rat liver was investigated by two independent methods, absorption and fluorescence spectroscopy. The increase in absorbance at 525 nm associated with Schiff’s base formation was used to investigate the binding of pyridoxal-5-P at a protein concentration of 1 X 10e5 M. A model based on two classes of independ...

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ژورنال

عنوان ژورنال: Bioorganic & Medicinal Chemistry Letters

سال: 2010

ISSN: 0960-894X

DOI: 10.1016/j.bmcl.2010.01.002