Reverse engineering: Transaminase biocatalyst development using ancestral sequence reconstruction

Matthew Wilding; Thomas S. Peat; Subha Kalyaanamoorthy; Janet Newman; Colin Scott; Lars S. Jermiin

doi:10.1039/c7gc02343j

Reverse engineering: Transaminase biocatalyst development using ancestral sequence reconstruction

Matthew Wilding^*, Thomas S. Peat, Subha Kalyaanamoorthy, Janet Newman, Colin Scott, Lars S. Jermiin

^*Corresponding author for this work

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

40 Citations (Scopus)

Abstract

The development of new biocatalysts using ancestral sequence reconstruction is reported. When applied to an ω-transaminase, the ancestral proteins demonstrated novel and superior activities with eighty percent of the forty compounds tested compared to the modern day protein, and improvements in activity of up to twenty fold. These included a range of compounds pertinent as feedstocks in polyamide manufacture.

Original language	English
Pages (from-to)	5375-5380
Number of pages	6
Journal	Green Chemistry
Volume	19
Issue number	22
DOIs	https://doi.org/10.1039/c7gc02343j
Publication status	Published - 2017

Access to Document

10.1039/c7gc02343j

Cite this

@article{c9cdc9d889e3487ab496ed541b88acda,

title = "Reverse engineering: Transaminase biocatalyst development using ancestral sequence reconstruction",

abstract = "The development of new biocatalysts using ancestral sequence reconstruction is reported. When applied to an ω-transaminase, the ancestral proteins demonstrated novel and superior activities with eighty percent of the forty compounds tested compared to the modern day protein, and improvements in activity of up to twenty fold. These included a range of compounds pertinent as feedstocks in polyamide manufacture.",

author = "Matthew Wilding and Peat, {Thomas S.} and Subha Kalyaanamoorthy and Janet Newman and Colin Scott and Jermiin, {Lars S.}",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2017.",

year = "2017",

doi = "10.1039/c7gc02343j",

language = "English",

volume = "19",

pages = "5375--5380",

journal = "Green Chemistry",

issn = "1463-9262",

publisher = "Royal Society of Chemistry",

number = "22",

}

TY - JOUR

T1 - Reverse engineering

T2 - Transaminase biocatalyst development using ancestral sequence reconstruction

AU - Wilding, Matthew

AU - Peat, Thomas S.

AU - Kalyaanamoorthy, Subha

AU - Newman, Janet

AU - Scott, Colin

AU - Jermiin, Lars S.

PY - 2017

Y1 - 2017

N2 - The development of new biocatalysts using ancestral sequence reconstruction is reported. When applied to an ω-transaminase, the ancestral proteins demonstrated novel and superior activities with eighty percent of the forty compounds tested compared to the modern day protein, and improvements in activity of up to twenty fold. These included a range of compounds pertinent as feedstocks in polyamide manufacture.

AB - The development of new biocatalysts using ancestral sequence reconstruction is reported. When applied to an ω-transaminase, the ancestral proteins demonstrated novel and superior activities with eighty percent of the forty compounds tested compared to the modern day protein, and improvements in activity of up to twenty fold. These included a range of compounds pertinent as feedstocks in polyamide manufacture.

UR - http://www.scopus.com/inward/record.url?scp=85034215072&partnerID=8YFLogxK

U2 - 10.1039/c7gc02343j

DO - 10.1039/c7gc02343j

M3 - Article

SN - 1463-9262

VL - 19

SP - 5375

EP - 5380

JO - Green Chemistry

JF - Green Chemistry

IS - 22

ER -

Reverse engineering: Transaminase biocatalyst development using ancestral sequence reconstruction

Abstract

Access to Document

Other files and links

Fingerprint

Cite this