Enzymatic transition states and transition state analogues

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

Transition states are the balance point of catalysis. Bonds are partially made and/or broken at the transition state, and the energy of the extended system provides near-equal probability that the system forms products or reverts to reactants. Enzymatic catalytic sites provide dynamic electronic environments that increase the probability that the transition state will be formed. Alignment of reactants in the Michaelis complex and motion of the catalytic site architecture are necessary to achieve the transition state. Transition state lifetimes are a fraction of a picosecond, preventing chemical equilibrium in extended covalent systems. Thus, dynamic descriptions of enzymatic transition states are required. Stable analogues similar to the transition state capture dynamic excursions that generate the transition state and convert them into thermodynamic binding energy. These analogues bind with extraordinary affinity relative to reactants.

Original languageEnglish (US)
Pages (from-to)604-613
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume15
Issue number6
DOIs
StatePublished - Dec 2005

Fingerprint

Catalytic Domain
Catalysis
Thermodynamics

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Enzymatic transition states and transition state analogues. / Schramm, Vern L.

In: Current Opinion in Structural Biology, Vol. 15, No. 6, 12.2005, p. 604-613.

Research output: Contribution to journalArticle

@article{fb4bb6a7dcae4ee791145133beef19f4,
title = "Enzymatic transition states and transition state analogues",
abstract = "Transition states are the balance point of catalysis. Bonds are partially made and/or broken at the transition state, and the energy of the extended system provides near-equal probability that the system forms products or reverts to reactants. Enzymatic catalytic sites provide dynamic electronic environments that increase the probability that the transition state will be formed. Alignment of reactants in the Michaelis complex and motion of the catalytic site architecture are necessary to achieve the transition state. Transition state lifetimes are a fraction of a picosecond, preventing chemical equilibrium in extended covalent systems. Thus, dynamic descriptions of enzymatic transition states are required. Stable analogues similar to the transition state capture dynamic excursions that generate the transition state and convert them into thermodynamic binding energy. These analogues bind with extraordinary affinity relative to reactants.",
author = "Schramm, {Vern L.}",
year = "2005",
month = "12",
doi = "10.1016/j.sbi.2005.10.017",
language = "English (US)",
volume = "15",
pages = "604--613",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - Enzymatic transition states and transition state analogues

AU - Schramm, Vern L.

PY - 2005/12

Y1 - 2005/12

N2 - Transition states are the balance point of catalysis. Bonds are partially made and/or broken at the transition state, and the energy of the extended system provides near-equal probability that the system forms products or reverts to reactants. Enzymatic catalytic sites provide dynamic electronic environments that increase the probability that the transition state will be formed. Alignment of reactants in the Michaelis complex and motion of the catalytic site architecture are necessary to achieve the transition state. Transition state lifetimes are a fraction of a picosecond, preventing chemical equilibrium in extended covalent systems. Thus, dynamic descriptions of enzymatic transition states are required. Stable analogues similar to the transition state capture dynamic excursions that generate the transition state and convert them into thermodynamic binding energy. These analogues bind with extraordinary affinity relative to reactants.

AB - Transition states are the balance point of catalysis. Bonds are partially made and/or broken at the transition state, and the energy of the extended system provides near-equal probability that the system forms products or reverts to reactants. Enzymatic catalytic sites provide dynamic electronic environments that increase the probability that the transition state will be formed. Alignment of reactants in the Michaelis complex and motion of the catalytic site architecture are necessary to achieve the transition state. Transition state lifetimes are a fraction of a picosecond, preventing chemical equilibrium in extended covalent systems. Thus, dynamic descriptions of enzymatic transition states are required. Stable analogues similar to the transition state capture dynamic excursions that generate the transition state and convert them into thermodynamic binding energy. These analogues bind with extraordinary affinity relative to reactants.

UR - http://www.scopus.com/inward/record.url?scp=27944458409&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=27944458409&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2005.10.017

DO - 10.1016/j.sbi.2005.10.017

M3 - Article

VL - 15

SP - 604

EP - 613

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

IS - 6

ER -