Abstract
Pyridoxal 5′-phosphate strongly and reversibly inhibited maize leaf 5-amino levulinic acid dehydratase. The inhibition was linearly competitive with respect to the substrate 5-aminolevulinic acid at pH values between 7 to 9.0. Pyridoxal was also effective as an inhibitor of the enzyme but pyridoxamine phosphate was not inhibitory. The results suggest that pyridoxal 5′-phosphate may be interacting with the enzyme either close to or at the 5-aminolevulinic acid binding site. This conclusion was further corroborated by the detection of a Schiff base between the enzyme and the substrate, 5-aminolevulinic acid and by reduction of pyridoxal phosphate and substrate complexes with sodium borohydride
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Abbreviations
- ALA-dehydratase:
-
5-Aminolevulinic acid dehydratase
- PALP:
-
pyridoxal 5′-phosphate
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Maralihalli, G.B., Bhagwat, A.S. Interaction of pyridoxal phosphate with the amino groups at the active site of 5- aminolevulinic acid dehydratase in maize. J. Biosci. 7, 359–364 (1985). https://doi.org/10.1007/BF02716797
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DOI: https://doi.org/10.1007/BF02716797