Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy-d-manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range-Reference-Cited by-同舟云学术

Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy-d-manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range

Published:2005-08 Issue:1 Volume:343 Page:35-47
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Li Zhili,Sau Apurba K.,Furdui Cristina M.,Anderson Karen S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference44 articles.

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3. Catalytic mechanism of 3-deoxy-d-manno-2-octulosonate-8-phosphate synthase. The use of synthetic analogues to probe the structure of the putative reaction intermediate;Baasov;Eur. J. Biochem.,1993

4. Mechanistic studies of 3-deoxy-d-manno-2-octulosonate-8-phosphate synthase from Escherichia coli;Kohen;Eur. J. Biochem.,1992

5. Catalytic mechanism of Kdo8P synthase: transient kinetic studies and evaluation of a putative reaction intermediate;Liang;Biochemistry,1998

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