jinghua qian

CHEMICAL MECHANISM OF HOMOCITRATE SYNTHASE FROM Saccharomyces cerevisiae

• Broschiertes Buch

Produktbeschreibung

Homocitrate synthase (HCS1) (acetyl-coenzyme A:
2-ketoglutarate C-transferase; E.C. 2.3.3.14)
catalyzes the first and regulated step in the
a-aminoadipate pathway for lysine synthesis.
The pH dependence of the kinetic parameters, isotope
effects, and dissociation constants for competitive
inhibitors are used to probe the chemical mechanism
of HCS. A general acid-base chemical mechanism is
proposed. site-directed mutagenesis was used to
change the three active site residues of HCS, and the
resulting mutant enzymes were characterized using
initial velocity studies, the pH dependence of the
kinetic parameters and isotope effects. Data
combined with a constant pH molecular dynamics
simulation study suggest a catalytic dyad, comprised
of Glu-155 and His-309, functions as a general base
to deprotonate the methyl group of AcCoA.

Produktdetails

• Verlag: VDM Verlag Dr. Müller
• Seitenzahl: 164
• Englisch
• Abmessung: 220mm
• ISBN-13: 9783639161557
• ISBN-10: 3639161556
• Artikelnr.: 26474996

Autorenporträt

Jinghua Qian had his Ph.D. degree in May,2008 from University of
Oklahoma. During that time, he worked with Dr. Paul F. Cook on
the chemical mechanism of homocitrate synthase from S.
cerevisiae. He was born in Liyang, Jiangsu, P.R. China. He
married to Jing Wen and has a son, James Z. Qian.