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

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

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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
Pages (from-to)69-73
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1119
Issue number1
DOIs
StatePublished - Feb 13 1992

Fingerprint

Esterases
Coenzyme A
NAD
Oxidoreductases
Aldehyde Dehydrogenase
Esters
Liver
Rats
Hydrolysis
Catalytic Domain
Substrates
Enzymes
4-nitrophenyl acetate

Keywords

  • 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

Cite this

Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase. / Popov, Kirill M.; Kedishvili, Natalia Y.; Harris, Robert.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1119, No. 1, 13.02.1992, p. 69-73.

Research output: Contribution to journalArticle

@article{bfbef330e7394f23ace61c04b3c49583,
title = "Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase",
abstract = "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.",
keywords = "Acetyl-CoA, Aldehyde dehydrogenase, Esterase, Malonate semialdehyde, Methylmalonate semialdehyde, Methylmalonate semialdehyde dehydrogenase, p-Nitrophenyl acetate",
author = "Popov, {Kirill M.} and Kedishvili, {Natalia Y.} and Robert Harris",
year = "1992",
month = "2",
day = "13",
doi = "10.1016/0167-4838(92)90236-7",
language = "English",
volume = "1119",
pages = "69--73",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase

AU - Popov, Kirill M.

AU - Kedishvili, Natalia Y.

AU - Harris, Robert

PY - 1992/2/13

Y1 - 1992/2/13

N2 - 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.

AB - 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.

KW - Acetyl-CoA

KW - Aldehyde dehydrogenase

KW - Esterase

KW - Malonate semialdehyde

KW - Methylmalonate semialdehyde

KW - Methylmalonate semialdehyde dehydrogenase

KW - p-Nitrophenyl acetate

UR - http://www.scopus.com/inward/record.url?scp=0026573355&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026573355&partnerID=8YFLogxK

U2 - 10.1016/0167-4838(92)90236-7

DO - 10.1016/0167-4838(92)90236-7

M3 - Article

VL - 1119

SP - 69

EP - 73

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -