Literature summary for 3.1.99.B1 extracted from

Matsui, E.; Musti, K.V.; Abe, J.; Yamasaki, K.; Matsui, I.; Harata, K.
Molecular structure and novel DNA binding sites located in loops of flap endonuclease-1 from Pyrococcus horikoshii (2002), J. Biol. Chem., 277, 37840-37847.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion, the crystal structure of flap endonuclease-1 from Pyrococcus horikoshii (phFEN-1) is determined to a resolution of 3.1 A	Pyrococcus horikoshii

Protein Variants

Protein Variants	Comment	Organism
K193A	KM-value is 4fold of the wild-type value, kcat is almost the same as for wild-type enzyme	Pyrococcus horikoshii
K193A/R194A/K195A	kcat/Km-value is decreased 76fold, compared with the value of wild-type enzyme	Pyrococcus horikoshii
K193A/R194A/K195A	the Km value of the mutant enzyme increases markedly and the kcat value decreases moderately	Pyrococcus horikoshii
K193E/R194E/K195E	the negatively charged triple mutant shows similar but more magnified effects on both parameters compared with the alanine triple mutant K193A/R194A/K195A	Pyrococcus horikoshii
K195A	KM-value is 8fold of the wild-type value, kcat is almost the same as for wild-type enzyme	Pyrococcus horikoshii
K199A	km and kcat values of the mutant enzyme differ little from the wild-type values	Pyrococcus horikoshii
K243A	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K243E	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K248A	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K249A	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K263A	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K263E	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii
K51E/R53E	the double mutant retains 30% of the wild-type kcat/Km value	Pyrococcus horikoshii
K87A	the kcat value of the mutant decreased 400fold, whereas the Km value is almost the same as that of wild-type enzyme	Pyrococcus horikoshii
K87A/R88A/K89A	the Km-value is 5fold higher, the kcat is 184fold lower than that of the wild-type enzyme	Pyrococcus horikoshii
K93A/R94A/R95A	Km-value and kcat-value is increased 17fold and decreased 96fold, respectively, compared with the wild-type values	Pyrococcus horikoshii
L47F	Km-value is similat to the value of the wild-type	Pyrococcus horikoshii
L47G	Km value of the mutant is increased 20fold	Pyrococcus horikoshii
R118A/K119A	kcat-value is decreased 111fold, compared with the wild-type value	Pyrococcus horikoshii
R118A/K119A	kcat/Km-value is decreased 1851fold, compared with the value of wild-type enzyme	Pyrococcus horikoshii
R118A/K119A	KM-value is magnified by 17fold	Pyrococcus horikoshii
R194A	KM-value is 5fold of the wild-type value, kcat is almost the same as for wild-type enzyme	Pyrococcus horikoshii
R40E/R42E	the Km of the mutynt is increased 105fold compared with wild-type. The kcat and kcat/Km values areo decreased 4- and 680fold, respectively	Pyrococcus horikoshii
R40G	Km of the mutant increases 7fold, compared with that of the wild-type enzyme	Pyrococcus horikoshii
R40G/R42G	kcat/Km-value is decreased 222fold, compared with the value of wild-type enzyme	Pyrococcus horikoshii
R40G/R42G	KM-value is magnified by 6fold	Pyrococcus horikoshii
R40G/R42G	Km-value of the mutant enzyme is elevated 26fold compared with that of the wild type	Pyrococcus horikoshii
R40Q	Km value of the single mutant enzyme increases 10fold	Pyrococcus horikoshii
R42E	Km and kcat/Km values of the mutant are 19fold higher and 25fold lower than the values of wild-type enzyme, respectively	Pyrococcus horikoshii
R42G	Km of the mutant increases 7fold, compared with that of the wild-type enzyme	Pyrococcus horikoshii
R42Q	KM-value is almost the same as the value for wild-type enzyme	Pyrococcus horikoshii
R88A	Km and kcat values of the mutant enzyme do not change markedly, compared with the wild-type values	Pyrococcus horikoshii
R89A	Km and kcat values of the mutant enzyme do not change markedly, compared with the wild-type values	Pyrococcus horikoshii
R94A	kcat-value is decreased 200fold compared with the wild-type value	Pyrococcus horikoshii
R94A	mutant enzyme shows a 12fold increase in the Km value and a 15fold decrease in the kcat-value compared with the wild-type values	Pyrococcus horikoshii
Y237A	Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values	Pyrococcus horikoshii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	comparison of the Km, kcat, and kcat/Km values between WT and the mutants	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O50123	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	comparison of the Km, kcat, and kcat/Km values between WT and the mutants	Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
additional information	-	additional information	comparison of the Km, kcat, and kcat/Km values between WT and the mutants	Pyrococcus horikoshii