Literature summary for 2.7.7.7 extracted from

Villbrandt, B.; Sobek, H.; Frey, B.; Schomburg, D.
Domain exchange: chimeras of Thermus aquaticus DNA polymerase, Escherichia coli DNA polymerase I and Thermotoga neapolitana DNA polymerase (2000), Protein Eng., 13, 645-654.

Search for more literature for 2.7.7.7

Cloned(Commentary)

Cloned (Comment)	Organism
expression of chimeric enzymes in Escherichia coli	Thermus aquaticus

Protein Variants

Protein Variants	Comment	Organism
additional information	the intervening domain of the thermostable Thermus aquaticus DNA polymerase (TAQ: polymerase), which has no catalytic activity, is exchanged for the 3'-5' exonuclease domain of the homologous mesophile Escherichia coli DNA polymerase I (Escherichia coli pol I) and the homologous thermostable Thermotoga neapolitana DNA polymerase (TNE: polymerase). Three chimeric DNA polymerases are constructed using the three-dimensional (3D) structure of the Klenow fragment of the Escherichia coli pol I and 3D models of the intervening and polymerase domains of the TAQ: polymerase and the TNE: polymerase: chimera TaqEc1 (exchange of residues 292-423 from TAQ: polymerase for residues 327-519 of Escherichia coli pol I), chimera TaqTne1 (exchange of residues 292-423 of TAQ: polymerase for residues 295-485 of TNE: polymerase) and chimera TaqTne2 (exchange of residues 292-448 of TAQ: polymerase for residues 295-510 of TNE: polymerase). The chimera TaqEc1 shows characteristics from both parental polymerases at an intermediate temperature of 50°C: high polymerase activity, processivity, 3'-5' exonuclease activity and proof-reading function The chimeras TaqTne1 and TaqTne2 show no significant 3'-5' exonuclease activity and no proof-reading function. The chimera TaqTne1 shows an optimum temperature at 60°C, decreased polymerase activity compared with the TAQ: polymerase and reduced processivity. The chimera TaqTne2 shows high polymerase activity at 72°C, processivity and less reduced thermostability compared with the chimera TaqTne1	Thermus aquaticus

Organism

Organism	UniProt	Comment	Textmining
Thermus aquaticus	P19821	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermus aquaticus

Synonyms

Synonyms	Comment	Organism
Taq polymerase	-	Thermus aquaticus

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Release 2023.1 (January 2023)