Metalloenzyme design and engineering through strategic modifications of native protein scaffolds

Igor D. Petrik, Jing Liu, Yi Lu

Research output: Contribution to journalReview article

Abstract

Metalloenzymes are among the major targets of protein design and engineering efforts aimed at attaining novel and efficient catalysis for biochemical transformation and biomedical applications, due to the diversity of functions imparted by the metallo-cofactors along with the versatility of the protein environment. Naturally evolved protein scaffolds can often serve as robust foundations for sustaining artificial active sites constructed by rational design, directed evolution, or a combination of the two strategies. Accumulated knowledge of structure-function relationship and advancement of tools such as computational algorithms and unnatural amino acids incorporation all contribute to the design of better metalloenzymes with catalytic properties approaching the needs of practical applications.

Original languageEnglish (US)
Pages (from-to)67-75
Number of pages9
JournalCurrent Opinion in Chemical Biology
Volume19
Issue number1
DOIs
StatePublished - Apr 1 2014

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Scaffolds
Protein Engineering
Catalysis
Catalytic Domain
Proteins
Amino Acids

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

Cite this

Metalloenzyme design and engineering through strategic modifications of native protein scaffolds. / Petrik, Igor D.; Liu, Jing; Lu, Yi.

In: Current Opinion in Chemical Biology, Vol. 19, No. 1, 01.04.2014, p. 67-75.

Research output: Contribution to journalReview article

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