case for monomeric Enzyme with intersubsite cooperativity

Name: case for monomeric Enzyme with intersubsite cooperativity
Brand: VDM Verlag
SKU: 9783639247039
Price: 17585 HUF
Availability: InStock

Szerző: Abdulkader Rahmo

Nyelv:

Kötés: Puha kötésű

Kiadó: VDM Verlag

Elérhetőség: Kiadói készleten rendelésre

Küldés 17-27 napon belül

17 585 Ft

This represents the thesis work dedicated to unraveling the underlying catalytic mechanism of the ex...

Információk a könyvről

Szerző

Abdulkader Rahmo

Nyelv

Angol

Kötés

Könyv - Puha kötésű

Kiadva

2010

oldal

EAN

9783639247039

ISBN

3639247035

Enbook ID

06832278

Kiadó

VDM Verlag

Súly

150

Méretek

152 x 229 x 6

Teljes leírás

This represents the thesis work dedicated to unraveling the underlying catalytic mechanism of the exopeptidase carboxypeptidase A. Earlier postulated mechanisms (by Cleland et.al., Lipscomb et.al., Suh et. al ), based on crystallographic and kinetic data, are experimentally and theoretically critically explored. Various synthetic (novel and past) substrates were used and studied by applying advanced kinetics. The synthesis of a novel substrate with unprecedented kinetic features (extreme kcat/Km value) assured excellent compatibility with the transition state structure of the enzyme; permitting the exclusion of several earlier proposed mechanisms. Multi- inhibitor analysis maps the likely location of substrates within this multi-subsite enzyme in the active catalytic state. Further, the study demonstrates a very early case of multi-subsite cooperative interaction in a monomeric enzyme. Later studies have substantiated this important aspect in other enzymes (FE: RNase A, 1999; phospholipase, 2001). It is currently believed that this is a common property of several enzymes and proteins that act on biopolymers and membrane lipids.

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case for monomeric Enzyme with intersubsite cooperativity

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