Literature summary for 3.1.21.10 extracted from

Nishino, T.; Komori, K.; Ishino, Y.; Morikawa, K.
Dissection of the regional roles of the archaeal Holliday junction resolvase Hjc by structural and mutational analyses (2001), J. Biol. Chem., 276, 35735-35740.

Search for more literature for 3.1.21.10

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzymes in Escherichia coli	Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment)	Organism
selenomethionine-containing enzyme crystallized by microbatch method with a silicone oil overlay, hexagonal form of the enzyme	Pyrococcus furiosus

Protein Variants

Protein Variants	Comment	Organism
D33A	mutant enzyme retains proper binding ablity to the Holliday junction	Pyrococcus furiosus
DELTA1-5	mutation causes a considerable decrease in Hjc-Holliday junction complex formation and cleavage activity	Pyrococcus furiosus
K30A/K31A	mutant enzyme retains proper binding ability to the Holliday junction, little or almost no cleavage activity	Pyrococcus furiosus
K51A/K52A	mutant enzyme retains proper binding ability to the Holliday junction, weak cleavage activity	Pyrococcus furiosus
R3A/K4A	mutation reduces the activity by 20fold as compared with the wild-type enzyme. The binding to the Holliday junction is substantially lowered	Pyrococcus furiosus

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA + H2O	Holliday junction cleavage using 4Jh and Z28	Pyrococcus furiosus	?	-	?

Synonyms

Synonyms	Comment	Organism
holliday junction resolvase hjc	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)