Single active‐site mutants are sufficient to enhance serine:pyruvate α‐transaminase activity in an ω‐transaminase

Single active‐site mutants are sufficient to enhance serine:pyruvate α‐transaminase activity in an ω‐transaminase

We have analyzed the natural evolution of transaminase structure and sequence between an α‐transaminase serine‐pyruvate aminotransferase and an ω‐transaminase from Chromobacterium violaceum with

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Bibliographische Detailangaben
Veröffentlicht in:The FEBS journal 2015-07, Vol.282 (13), p.2512-2526
Hauptverfasser: Deszcz, Dawid, Affaticati, Pierre, Ladkau, Nadine, Gegel, Alex, Ward, John M, Hailes, Helen C, Dalby, Paul A
Format: Artikel
Sprache:eng
Schlagworte:
active sites
aminotransferase
biocatalysis
Catalytic Domain
Chromobacterium violaceum
directed evolution
engineering
evolution
High-Throughput Screening Assays
Hydrogen Bonding
Models, Molecular
mutants
Mutation
Phylogeny
sequence analysis
Substrate Specificity
transaminase
transaminases
Transaminases - chemistry
Transaminases - metabolism
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Beschreibung
Zusammenfassung:We have analyzed the natural evolution of transaminase structure and sequence between an α‐transaminase serine‐pyruvate aminotransferase and an ω‐transaminase from Chromobacterium violaceum with
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.13293