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Redesign of substra...
Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation
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- Nilsson, LO (författare)
- Uppsala universitet,Institutionen för naturvetenskaplig biokemi
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Gustafsson, A (författare)
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Mannervik, B (författare)
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(creator_code:org_t)
- NATL ACAD SCIENCES, 2000
- 2000
- Engelska.
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Ingår i: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. - : NATL ACAD SCIENCES. - 0027-8424. ; 97:17, s. 9408-9412
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- The evolution of proteins for novel functions involves point mutations and recombinations of domains or structural segments. Mimicking this process by rational design in vitro is still a major challenge. The present report demonstrates that the active sit
Nyckelord
- hydroxyalkenal; protein redesign; sequential design; S-TRANSFERASES; ACTIVE-SITE; HETEROLOGOUS EXPRESSION; COENZYME SPECIFICITY; EVOLUTION; ACID; DEHYDROGENASE; ENZYME; DETOXICATION; MUTAGENESIS
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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