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

BRENDA support

Literature summary for 3.4.19.1 extracted from

  • Zhou, X.; Wang, H.; Zhang, Y.; Gao, L.; Feng, Y.
    Alteration of substrate specificities of thermophilic alpha/beta hydrolases through domain swapping and domain interface optimization (2012), Acta Biochim. Biophys. Sin., 44, 965-973.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli of of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1 Aeropyrum pernix

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
wild-type enzyme Aeropyrum pernix

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
60 80 60°C: about 40% of maximal activity, 80°C: optimum Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
wild-type enzyme Aeropyrum pernix

pH Range

pH Minimum pH Maximum Comment Organism
7.5 9.5 pH 7.5: about 50% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme Aeropyrum pernix