Literature summary for 4.1.99.2 extracted from
Kim, J.H.; Song, J.J.; Kim, B.G.; Sung, M.H.; Lee, S.C.
Enhanced stability of tyrosine phenol-lyase from Symbiobacterium toebii by DNA shuffling (2004), J. Microbiol. Biotechnol., 14, 153-157.
No PubMed abstract available
Protein Variants
Protein Variants |
Comment |
Organism |
A13V |
mutant exhibits higher temperature and denaturant stability than wild-type enzyme |
Symbiobacterium toebii |
General Stability
General Stability |
Organism |
mutant enzyme A13V loses 50% of its catalytic activity in 3 M urea, wild-type enzyme completely loses activity |
Symbiobacterium toebii |
Organism
Organism |
UniProt |
Comment |
Textmining |
Symbiobacterium toebii |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
mutant enzyme A13V |
Symbiobacterium toebii |