Literature summary for 4.1.99.1 extracted from

Kudo, H.; Natsume, R.; Nishiyama, M.; Horinouchi, S.
Analysis of stability and catalytic properties of two tryptophanases from a thermophile (1999), Protein Eng., 12, 687-692.

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Protein Variants

Protein Variants	Comment	Organism
M383I	Tna2, slight increase of catalytic activity	Symbiobacterium thermophilum
additional information	chimeric forms of Tna1/Tna2, thermal stability increases as the contnent of the N-terminal portion of Tna1 in the chimera increases	Symbiobacterium thermophilum
S395G	Tna2, slight increase of catalytic activity	Symbiobacterium thermophilum
V382M	Tna2, slight reduction of catalytic activity	Symbiobacterium thermophilum
V382M/M383I/S395G	Tna2, 2fold increase in catalytic activity	Symbiobacterium thermophilum

Organism

Organism	UniProt	Comment	Textmining
Symbiobacterium thermophilum	-	isoforms Tna1, Tna2	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
80	-	5 min, Tna1 retains alomost complete activity, Tna2 is inactivated	Symbiobacterium thermophilum
90	-	5 min, Tna1 retains more than 70% of activity, Tna2 is inactivated	Symbiobacterium thermophilum

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Release 2023.1 (January 2023)