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Titolo:
ENZYMATIC TRANSITION-STATES AND TRANSITION-STATE ANALOG DESIGN
Autore:
SCHRAMM VL;
Indirizzi:
YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT BIOCHEM,1300 MORRIS PK AVEBRONX NY 10461
Titolo Testata:
Annual review of biochemistry
, volume: 67, anno: 1998,
pagine: 693 - 720
SICI:
0066-4154(1998)67:<693:ETATAD>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PURINE NUCLEOSIDE PHOSPHORYLASE; ADENOSINE-MONOPHOSPHATE NUCLEOSIDASE; NICOTINAMIDE ADENINE-DINUCLEOTIDE; ELECTROSTATIC POTENTIAL SURFACE; S-ADENOSYLMETHIONINE SYNTHETASE; LIVER ALCOHOL-DEHYDROGENASE; AMP NUCLEOSIDASE; CRYSTAL-STRUCTURE; OROTATE PHOSPHORIBOSYLTRANSFERASE; CRITHIDIA-FASCICULATA;
Keywords:
CATALYSIS; ISOTOPE EFFECTS; INHIBITOR; ENZYMES; INHIBITOR DESIGN;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
117
Recensione:
Indirizzi per estratti:
Citazione:
V.L. Schramm, "ENZYMATIC TRANSITION-STATES AND TRANSITION-STATE ANALOG DESIGN", Annual review of biochemistry, 67, 1998, pp. 693-720

Abstract

All chemical transformations pass through an unstable structure called the transition state, which is poised between the chemical structures of the substrates and products. The transition states for chemical reactions are proposed to have lifetimes near 10(-13 sec), the time fora single bond vibration, No physical or spectroscopic method is available to directly observe the structure of the transition state for enzymatic reactions, Yet transition state structure is central to understanding catalysis, because enzymes function by lowering activation energy. An accepted view of enzymatic catalysis is tight binding to the unstable transition state structure, Transition state mimics bind tightly to enzymes by capturing a fraction of the binding energy for the transition state species. The identification of numerous transition stateinhibitors supports the transition state stabilization hypothesis forenzymatic catalysis. Advances in methods for measuring and interpreting kinetic isotope effects and advances in computational chemistry have provided an experimental route to understand transition state structure, Systematic analysis of intrinsic kinetic isotope effects providesgeometric and electronic structure for enzyme-bound transition states. This information has been used to compare transition states for chemical and enzymatic reactions; determine whether enzymatic activators alter transition state structure; design transition state inhibitors; and provide the basis for predicting the affinity of enzymatic inhibitors. Enzymatic transition states provide an understanding of catalysis and permit the design of transition state inhibitors. This article reviews transition state theory for enzymatic reactions, Selected examples of enzymatic transition states are compared to the respective transition state inhibitors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/10/20 alle ore 10:39:32