Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.62 extracted from

  • Zhou, K.; Dong, Y.; Zheng, H.; Chen, B.; Mao, R.; Zhou, L.; Wang, Y.
    Expression, fermentation, purification and lyophilisation of recombinant subtilisin QK in Pichia pastoris (2017), Process Biochem., 54, 1-8 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the codon-optimized gene encoding enzyme subtilisin QK in Pichia pastoris strain GS115, the thrombolytic activity of QK reaches 112000 IU (urokinase unit) per ml and the specific activity is 14,679 IU/mg under optimal culture and fermentation conditions, method optimization, detailed overview Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q7WVA6
-
-
Bacillus subtilis QK02 Q7WVA6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information performance of a thrombolytic activity assay Bacillus subtilis ?
-
?
additional information performance of a thrombolytic activity assay Bacillus subtilis QK02 ?
-
?

Synonyms

Synonyms Comment Organism
subtilisin QK
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
thrombolytic activity assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
thrombolytic activity assay at Bacillus subtilis

General Information

General Information Comment Organism
evolution subtilisin QK is highly homologous to nattokinase (NK, Q548F3) Bacillus subtilis