PMID:7848266: Difference between revisions

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<span style = 'font-size: large'> '''Bornemann, S, Balasubramanian, S, Coggins, JR, Abell, C, Lowe, DJ and Thorneley, RN'''  (1995) Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect under single-turnover and steady-state conditions shows that a flavin intermediate forms before the C-(6proR)-H bond is cleaved.''Biochem. J.'' '''305 ( Pt 3)''':707-10</span>
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'''Bornemann, S, Balasubramanian, S, Coggins, JR, Abell, C, Lowe, DJ and Thorneley, RN'''  (1995) Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect under single-turnover and steady-state conditions shows that a flavin intermediate forms before the C-(6proR)-H bond is cleaved. ''Biochem. J.'' '''305 ( Pt 3)''':707-10
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!align=left  |Abstract
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We report the observation of a deuterium kinetic isotope effect for the conversion of 5-enolpyruvylshikimate-3-phosphate into chorismate (6proR2HV = 1.13 +/- 0.03) using recombinant chorismate synthase from Escherichia coli. Similar isotope effects were observed for the decay of a spectroscopically characterized flavin intermediate (6proR2Hk = 1.17 +/- 0.04) during single-turnover experiments. The main rate-limiting steps and C-(6proR)-H bond breaking are therefore distinct and both must occur after the formation of the flavin intermediate and either before or concomitant with its decay.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7848266 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1136315 PMC1136315]


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|{{TableHeadingColor}} |'''Abstract''' || We report the observation of a deuterium kinetic isotope effect for the conversion of 5-enolpyruvylshikimate-3-phosphate into chorismate (6proR2HV = 1.13 +/- 0.03) using recombinant chorismate synthase from Escherichia coli. Similar isotope effects were observed for the decay of a spectroscopically characterized flavin intermediate (6proR2Hk = 1.17 +/- 0.04) during single-turnover experiments. The main rate-limiting steps and C-(6proR)-H bond breaking are therefore distinct and both must occur after the formation of the flavin intermediate and either before or concomitant with its decay.
!align=left  |Keywords
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Binding Sites; Chorismic Acid/metabolism; Deuterium; Escherichia coli/enzymology; Flavins/metabolism; Hydrogen Bonding; Kinetics; Lyases/metabolism; Phosphorus-Oxygen Lyases; Recombinant Proteins/metabolism; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism; Spectrophotometry
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7848266 PubMed]
 
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Latest revision as of 04:51, 15 September 2013

Citation

Bornemann, S, Balasubramanian, S, Coggins, JR, Abell, C, Lowe, DJ and Thorneley, RN (1995) Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect under single-turnover and steady-state conditions shows that a flavin intermediate forms before the C-(6proR)-H bond is cleaved. Biochem. J. 305 ( Pt 3):707-10

Abstract

We report the observation of a deuterium kinetic isotope effect for the conversion of 5-enolpyruvylshikimate-3-phosphate into chorismate (6proR2HV = 1.13 +/- 0.03) using recombinant chorismate synthase from Escherichia coli. Similar isotope effects were observed for the decay of a spectroscopically characterized flavin intermediate (6proR2Hk = 1.17 +/- 0.04) during single-turnover experiments. The main rate-limiting steps and C-(6proR)-H bond breaking are therefore distinct and both must occur after the formation of the flavin intermediate and either before or concomitant with its decay.

Links

PubMed PMC1136315

Keywords

Binding Sites; Chorismic Acid/metabolism; Deuterium; Escherichia coli/enzymology; Flavins/metabolism; Hydrogen Bonding; Kinetics; Lyases/metabolism; Phosphorus-Oxygen Lyases; Recombinant Proteins/metabolism; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism; Spectrophotometry

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