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Metal Ion Inhibition of Nonenzymatic Pyridoxal Phosphate Catalyzed Decarboxylation and Transamination

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    Metal Ion Inhibition of Nonenzymatic Pyridoxal Phosphate Catalyzed Decarboxylation and Transamination
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    Contribution from the Department of Chemistry, University of CaliforniaDavis, One Shields Avenue, Davis, California 95616
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2001, 123, 2, 193–198
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    https://doi.org/10.1021/ja0026354
    Published December 19, 2000
    Copyright © 2001 American Chemical Society
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    Abstract

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    Nonenzymatic pyridoxal phosphate (PLP) catalyzed decarboxylations and transaminations have been revisited experimentally. Metal ions are known to catalyze a variety of PLP-dependent reactions in solution, including transamination. It is demonstrated here that the rate accelerations previously observed are due solely to enhancement of Schiff base formation under subsaturating conditions. A variety of metal ions were tested for their effects on the reactivity of the 2-methyl-2-aminomalonate Schiff bases. All were found to have either no effect or a small inhibitory one. The effects of Al3+ were studied in detail with the Schiff bases of 2-methyl-2-aminomalonate, 2-aminoisobutyrate, alanine, and ethylamine. The decarboxylation of 2-methyl-2-aminomalonate is unaffected by metalation with Al3+, while the decarboxylation of 2-aminoisobutyrate is inhibited 125-fold. The transamination reaction of ethylamine is 75-fold slower than that of alanine. Ethylamine transamination is inhibited 4-fold by Al3+ metalation, while alanine transamination is inhibited only 1.3-fold. Metal ion inhibition of Schiff base reactivity suggests a simple explanation for the lack of known PLP dependent enzymes that make direct mechanistic use of metal ions. A comparison of enzyme catalyzed, PLP catalyzed, and uncatalyzed reactions shows that PLP dependent decarboxylases are among the best known biological rate enhancers:  decarboxylation occurs 1018-fold faster on the enzyme surface than it does free in solution. PLP itself provides the lion's share of the catalytic efficiency of the holoenzyme:  at pH 8, free PLP catalyzes 2-aminoisobutyrate decarboxylation by ∼1010-fold, with the enzyme contributing an additional ∼108-fold.

    Copyright © 2001 American Chemical Society

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     To whom correspondence should be addressed. E-mail:  toney@ chem.ucdavis.edu. Phone:  (530) 754-5282. Fax:  (530) 752-8995.

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    Cite this: J. Am. Chem. Soc. 2001, 123, 2, 193–198
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja0026354
    Published December 19, 2000
    Copyright © 2001 American Chemical Society
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