The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

Vanja Stojković; Laura L. Perissinotti; Jeeyeon Lee; Stephen J. Benkovic; Amnon Kohen

doi:10.1039/c0cc02988b

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

Vanja Stojković, Laura L. Perissinotti, Jeeyeon Lee, Stephen J. Benkovic, Amnon Kohen

Chemistry

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

Original language	English (US)
Pages (from-to)	8974-8976
Number of pages	3
Journal	Chemical Communications
Volume	46
Issue number	47
DOIs	https://doi.org/10.1039/c0cc02988b
State	Published - Dec 21 2010

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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10.1039/c0cc02988b

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title = "The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer",

abstract = "Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.",

author = "Vanja Stojkovi{\'c} and Perissinotti, {Laura L.} and Jeeyeon Lee and Benkovic, {Stephen J.} and Amnon Kohen",

year = "2010",

month = dec,

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doi = "10.1039/c0cc02988b",

language = "English (US)",

volume = "46",

pages = "8974--8976",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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T1 - The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

AU - Stojković, Vanja

AU - Perissinotti, Laura L.

AU - Lee, Jeeyeon

AU - Benkovic, Stephen J.

AU - Kohen, Amnon

PY - 2010/12/21

Y1 - 2010/12/21

N2 - Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

AB - Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

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U2 - 10.1039/c0cc02988b

DO - 10.1039/c0cc02988b

M3 - Article

C2 - 20972508

AN - SCOPUS:78649358299

SN - 1359-7345

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SP - 8974

EP - 8976

JO - Chemical Communications

JF - Chemical Communications

IS - 47

ER -

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

Abstract

All Science Journal Classification (ASJC) codes

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