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Conformational changes and loose packing promote E. coli Tryptophanase cold lability
BACKGROUND: Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through an enamine bond to Lys...
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| Hoofdauteurs: | , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
BioMed Central
2009
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2770544/ https://ncbi.nlm.nih.gov/pubmed/19814824 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1472-6807-9-65 |
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