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

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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

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Release 2023.1 (January 2023)