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Literature summary for 3.4.21.81 extracted from

  • Joe, K.; Borgford, T.J.; Bennet, A.J.
    Generation of a thermostable and denaturant-resistant peptide ligase (2004), Biochemistry, 43, 7672-7677.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S195A/T213L/F228H i.e. streptoligase, catalyzes peptide ligation efficiently. Ligation proceeds via an acyl-enzyme intermediate involving H57. Mutant exhibits half-life for unfolding of 16.3 min at 55°C in the absence of stabilizing substrates Streptomyces griseus

Organism

Organism UniProt Comment Textmining
Streptomyces griseus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Sc-AAPF-p-nitroanilide + H2O
-
Streptomyces griseus ?
-
?
Sc-AAPF-SBn + FAASF-NH2
-
Streptomyces griseus ? ligation to nonapeptide by mutant S195A/T213L/F228H ?
Sc-AAPF-SBn + H2O
-
Streptomyces griseus ?
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
ratio of ligation to hydrolysis by mutant S195A/T213L/F228H decreases with increase in temperature from 30°C to 60°C Streptomyces griseus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
mutant S195A/T213L/F228H, half-life for unfolding of 16.3 min in the absence of stabilizing substrates Streptomyces griseus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
hydrolysis reaction Streptomyces griseus
8.8 9.2 ligation reaction of mutant S195A/T213L/F228H Streptomyces griseus