Literature summary for 1.1.5.2 extracted from

Sode, K.; Ootera, T.; Shirahane, M.; Witarto, A.B.; Igarashi, S.; Yoshida, H.
Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement (2000), Enzyme Microb. Technol., 26, 491-496.

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Application

Application	Comment	Organism
analysis	application of mutant enzyme S231K as a glucose sensor constituent. The mutant has more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme and retains catalytic activity similar to the wild-type enzyme	Acinetobacter calcoaceticus

Protein Variants

Protein Variants	Comment	Organism
S231C	increase in thermal stability	Acinetobacter calcoaceticus
S231D	increase in thermal stability	Acinetobacter calcoaceticus
S231H	increase in thermal stability	Acinetobacter calcoaceticus
S231K	more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme, retains catalytic activity similar to the wild-type enzyme	Acinetobacter calcoaceticus
S231L	increase in thermal stability	Acinetobacter calcoaceticus
S231M	increase in thermal stability	Acinetobacter calcoaceticus
S231N	increase in thermal stability	Acinetobacter calcoaceticus

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter calcoaceticus	-	-	-

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Release 2023.1 (January 2023)