PMID:2407239: Difference between revisions

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<span style = 'font-size: large'> '''Hawkes, TR, Lewis, T, Coggins, JR, Mousdale, DM, Lowe, DJ and Thorneley, RN'''  (1990) Chorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate.''Biochem. J.'' '''265''':899-902</span>
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!align=left  |Citation
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'''Hawkes, TR, Lewis, T, Coggins, JR, Mousdale, DM, Lowe, DJ and Thorneley, RN'''  (1990) Chorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate. ''Biochem. J.'' '''265''':899-902
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!align=left  |Abstract
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The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of this result for the mechanism of action of chorismate synthase are discussed.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2407239 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1133717 PMC1133717]


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|{{TableHeadingColor}} |'''Abstract''' || The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of this result for the mechanism of action of chorismate synthase are discussed.
!align=left  |Keywords
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Binding Sites; Chemical Phenomena; Chemistry; Escherichia coli/enzymology; Kinetics; Lyases/metabolism; Phosphates/metabolism; Phosphorus-Oxygen Lyases; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2407239 PubMed]
 
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Latest revision as of 04:44, 15 September 2013

Citation

Hawkes, TR, Lewis, T, Coggins, JR, Mousdale, DM, Lowe, DJ and Thorneley, RN (1990) Chorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate. Biochem. J. 265:899-902

Abstract

The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of this result for the mechanism of action of chorismate synthase are discussed.

Links

PubMed PMC1133717

Keywords

Binding Sites; Chemical Phenomena; Chemistry; Escherichia coli/enzymology; Kinetics; Lyases/metabolism; Phosphates/metabolism; Phosphorus-Oxygen Lyases; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism

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