Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules.

Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Research Abstract Details 

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Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Abstract Text:

Mbako R Nnyepi,Yi Peng,Joan B Broderick,

Escherichia coli AdhE has been reported to harbor three distinct enzymatic activities: alcohol dehydrogenase, acetaldehyde-CoA dehydrogenase, and pyruvate formate-lyase (PFL) deactivase. Herein we report on the cloning, expression, and purification of E. coli AdhE, and the re-investigation of its purported enzymatic activities. While both the alcohol dehydrogenase and acetaldehyde-CoA dehydrogenase activities were readily detectable, we were unable to obtain any evidence for catalytic deactivation of PFL by AdhE, regardless of whether the reported cofactors for deactivation (Fe(II), NAD, and CoA) were present. Our results demonstrate that AdhE is not a PFL deactivating enzyme. We have also examined the potential for deactivation of active PFL by small-molecule thiols. Both beta-mercaptoethanol and dithiothreitol deactivate PFL efficiently, with the former providing quite rapid deactivation. PFL deactivated by these thiols can be reactivated, suggesting that this deactivation is non-destructive transfer of an H atom equivalent to quench the glycyl radical.

Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Publishing Authors By Initials

MR Nnyepi,Y Peng,JB Broderick,

For similar macromolecular substances: multiprotein complexes: multienzyme complexes research abstracts see: macromolecular substances: multiprotein complexes: multienzyme complexes research

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Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Archives of biochemistry and biophysics

VOLUME: 459

Page Numbers: 1-9

Journal Abbreviation: Arch. Biochem. Biophys.

ISSN: 0003-9861

DAY: 12

MONTH: 01

YEAR: 2007

Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372430

Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Keywords Mesh Terms:

KEYWORDS: Multienzyme Complexes

MESH TERMS: chemistry

Chemical & Substance for Abstract: Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Information

Substance Name: formate C-acetyltransferase

Registry Number: EC 2.3.1.54

Grant and Affiliation Information for Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules.

AFFILIATION: Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59718, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM054608-10

ACRONYM: GM

MEDLINETA: Arch Biochem Biophys

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