Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase

Kirill M. Popov, Natalia Y. Kedishvili, Robert A. Harris

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Methylmalonate semialdehyde dehydrogenase purified to homogeneity from rat liver possesses, in addition to its coupled aldehyde dehydrogenase and CoA ester synthetic activity, the ability to hydrolyze p-nitrophenyl acetate. The following observations suggest that this activity is an active site phenomenon: (a) p-nitrophenyl acetate hydrolysis was inhibited by malonate semialdehyde, substrate for the dehydrogenase reaction; (b) p-nitrophenyl acetate was a strong competitive inhibitor of the dehydrogenase activity; (c) NAD+ and NADH activated the esterase activity; (d) coenzyme A, acceptor of acyl groups in the dehydrogenase reaction, accelerated the esterase activity; and (e) the product of the esterase reaction proceeding in the presence of coenzyme A was acety;-CoA. These findings suggest that an S-acyl enzyme (thioester intermediate) is likely common to both the esterase reaction and the aldehyde dehydrogenase/CoA ester synthetic reaction.

Original languageEnglish (US)
Pages (from-to)69-73
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number1
StatePublished - Feb 13 1992


  • Acetyl-CoA
  • Aldehyde dehydrogenase
  • Esterase
  • Malonate semialdehyde
  • Methylmalonate semialdehyde
  • Methylmalonate semialdehyde dehydrogenase
  • p-Nitrophenyl acetate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Fingerprint Dive into the research topics of 'Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase'. Together they form a unique fingerprint.

Cite this