Active site generated analogs of reactive intermediates in enzymic reactions. Potent inhibition of pyruvate dehydrogenase by a phosphonate analog of pyruvate
R Kluger, DC Pike - Journal of the American Chemical Society, 1977 - ACS Publications
R Kluger, DC Pike
Journal of the American Chemical Society, 1977•ACS PublicationsOO IIII PDH-TPP· CH3CP xoch3 f1 OH 0 Me I+. Tii 0" 5= t PDH· XZ^ C—C—P(2)/-*< k XCH·
reaction conditions (eq 2). We now find that MAP does com-pete with pyruvate for the active
site of Ei of PDH. The magnitude and specificity of inhibition suggest a common type of
covalent adduct forms. The involvement of TPP in the overall PDH reaction suggests the
nature of the addition product.
reaction conditions (eq 2). We now find that MAP does com-pete with pyruvate for the active
site of Ei of PDH. The magnitude and specificity of inhibition suggest a common type of
covalent adduct forms. The involvement of TPP in the overall PDH reaction suggests the
nature of the addition product.
OO IIII PDH-TPP· CH3CP xoch3 f1 OH 0 Me I+. Tii 0" 5= t PDH· XZ^ C—C—P(2)/-*< k XCH· reaction conditions (eq 2). We now find that MAP does com-pete with pyruvate for the active site of Ei of PDH. The magnitude and specificity of inhibition suggest a common type of covalent adduct forms. The involvement of TPP in the overall PDH reaction suggests the nature of the addition product.
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