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. 1977 Aug 1;165(2):409-11.
doi: 10.1042/bj1650409.

Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase

J M La Nauze, J R Coggins, H B Dixon

Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase

J M La Nauze et al. Biochem J. .

Abstract

Phosphonoacetaldehyde hydrolase (EC 3.11.1.1), the bacterial enzyme that catalyses the reaction HCO-CH2-PO(OH)2+H2O leads to HCO-CH3+Pi, is inactivated by borohydride if either phosphonoacetaldehyde or acetaldehyde is present. This supports the suggestion that the substrate forms an imine with an amino group of the enzyme. Such imine formation would labilize the C-P bond in the same way that aldolase and related enzymes labilize C-C and C-H bonds (Scheme 1a).

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References

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