The In Situ Enzymatic Screening (ISES) Approach to Reaction Discovery and Catalyst Identification

Robert A. Swyka, David B Berkowitz

Research output: Contribution to journalArticle

Abstract

The importance of discovering new chemical transformations and/or optimizing catalytic combinations has led to a flurry of activity in reaction screening. The in situ enzymatic screening (ISES) approach described here utilizes biological tools (enzymes/cofactors) to advance chemistry. The protocol interfaces an organic reaction layer with an adjacent aqueous layer containing reporting enzymes that act upon the organic reaction product, giving rise to a spectroscopic signal. ISES allows the experimentalist to rapidly glean information on the relative rates of a set of parallel organic/organometallic reactions under investigation, without the need to quench the reactions or draw aliquots. In certain cases, the real-time enzymatic readout also provides information on sense and magnitude of enantioselectivity and substrate specificity. This article contains protocols for single-well (relative rate) and double-well (relative rate/enantiomeric excess) ISES, in addition to a colorimetric ISES protocol and a miniaturized double-well procedure.

Original languageEnglish (US)
Pages (from-to)285-305
Number of pages21
JournalCurrent protocols in chemical biology
Volume9
Issue number4
DOIs
StatePublished - Dec 14 2017

Fingerprint

Coenzymes
Substrate Specificity
Enzymes

Keywords

  • catalysis
  • enzymatic screening
  • metal-ligand combinations
  • reaction discovery
  • UV/vis spectrophotometry

ASJC Scopus subject areas

  • Medicine(all)

Cite this

The In Situ Enzymatic Screening (ISES) Approach to Reaction Discovery and Catalyst Identification. / Swyka, Robert A.; Berkowitz, David B.

In: Current protocols in chemical biology, Vol. 9, No. 4, 14.12.2017, p. 285-305.

Research output: Contribution to journalArticle

@article{3bf734becc5c443f9812d4430eb612c0,
title = "The In Situ Enzymatic Screening (ISES) Approach to Reaction Discovery and Catalyst Identification",
abstract = "The importance of discovering new chemical transformations and/or optimizing catalytic combinations has led to a flurry of activity in reaction screening. The in situ enzymatic screening (ISES) approach described here utilizes biological tools (enzymes/cofactors) to advance chemistry. The protocol interfaces an organic reaction layer with an adjacent aqueous layer containing reporting enzymes that act upon the organic reaction product, giving rise to a spectroscopic signal. ISES allows the experimentalist to rapidly glean information on the relative rates of a set of parallel organic/organometallic reactions under investigation, without the need to quench the reactions or draw aliquots. In certain cases, the real-time enzymatic readout also provides information on sense and magnitude of enantioselectivity and substrate specificity. This article contains protocols for single-well (relative rate) and double-well (relative rate/enantiomeric excess) ISES, in addition to a colorimetric ISES protocol and a miniaturized double-well procedure.",
keywords = "catalysis, enzymatic screening, metal-ligand combinations, reaction discovery, UV/vis spectrophotometry",
author = "Swyka, {Robert A.} and Berkowitz, {David B}",
year = "2017",
month = "12",
day = "14",
doi = "10.1002/cpch.30",
language = "English (US)",
volume = "9",
pages = "285--305",
journal = "Current protocols in chemical biology",
issn = "2160-4762",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - The In Situ Enzymatic Screening (ISES) Approach to Reaction Discovery and Catalyst Identification

AU - Swyka, Robert A.

AU - Berkowitz, David B

PY - 2017/12/14

Y1 - 2017/12/14

N2 - The importance of discovering new chemical transformations and/or optimizing catalytic combinations has led to a flurry of activity in reaction screening. The in situ enzymatic screening (ISES) approach described here utilizes biological tools (enzymes/cofactors) to advance chemistry. The protocol interfaces an organic reaction layer with an adjacent aqueous layer containing reporting enzymes that act upon the organic reaction product, giving rise to a spectroscopic signal. ISES allows the experimentalist to rapidly glean information on the relative rates of a set of parallel organic/organometallic reactions under investigation, without the need to quench the reactions or draw aliquots. In certain cases, the real-time enzymatic readout also provides information on sense and magnitude of enantioselectivity and substrate specificity. This article contains protocols for single-well (relative rate) and double-well (relative rate/enantiomeric excess) ISES, in addition to a colorimetric ISES protocol and a miniaturized double-well procedure.

AB - The importance of discovering new chemical transformations and/or optimizing catalytic combinations has led to a flurry of activity in reaction screening. The in situ enzymatic screening (ISES) approach described here utilizes biological tools (enzymes/cofactors) to advance chemistry. The protocol interfaces an organic reaction layer with an adjacent aqueous layer containing reporting enzymes that act upon the organic reaction product, giving rise to a spectroscopic signal. ISES allows the experimentalist to rapidly glean information on the relative rates of a set of parallel organic/organometallic reactions under investigation, without the need to quench the reactions or draw aliquots. In certain cases, the real-time enzymatic readout also provides information on sense and magnitude of enantioselectivity and substrate specificity. This article contains protocols for single-well (relative rate) and double-well (relative rate/enantiomeric excess) ISES, in addition to a colorimetric ISES protocol and a miniaturized double-well procedure.

KW - catalysis

KW - enzymatic screening

KW - metal-ligand combinations

KW - reaction discovery

KW - UV/vis spectrophotometry

UR - http://www.scopus.com/inward/record.url?scp=85038934729&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85038934729&partnerID=8YFLogxK

U2 - 10.1002/cpch.30

DO - 10.1002/cpch.30

M3 - Article

VL - 9

SP - 285

EP - 305

JO - Current protocols in chemical biology

JF - Current protocols in chemical biology

SN - 2160-4762

IS - 4

ER -