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Literature summary for 3.1.99.B3 extracted from

  • Komori, K.; Fujikane, R.; Shinagawa, H.; Ishino, Y.
    Novel endonuclease in Archaea cleaving DNA with various branched structure (2002), Genes Genet. Syst., 77, 227-241.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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Purification (Commentary)

Purification (Comment) Organism
full-length Hef protein can not be produced in Escherichia coli. The gene for the N-terminal domain (Met1-Ala546) is easily cloned into the same vector. The gene product is designated as N546. The cloning of the gene for the C-terminal domain (Gln547-Glu763) into the same expression vector is difficult. One clone is obtained, however, the plasmid from the clone contains a single base substitution, which causes a single base substitution, which causes a single amino acid change from Phe to Leu. The mutant protein has the same cleavage specificity and is designated C547' Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structure-specific endonuclease cleaving the DNA strand at the 5'-side of nicked or flapped positions in the duplex DNA Pyrococcus furiosus ?
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?

Synonyms

Synonyms Comment Organism
HEF
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Pyrococcus furiosus
helicase-associated endonuclease for fork-structured DNA
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Pyrococcus furiosus

General Information

General Information Comment Organism
physiological function may be a prototypical enzyme for resolving stalled forks during DNA replication, as well as working at nucleotide excision repair Pyrococcus furiosus