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Literature summary for 4.1.99.3 extracted from

  • McLeod, N.R.; Brolich, M.A.; Damiani, M.J.; ONeill, M.A.
    Distinct recognition loop dynamics in cryptochrome-DASH and photolyase revealed by limited proteolysis (2009), Biochem. Biophys. Res. Commun., 385, 424-429.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
untagged photolyase overexpressed from pET3a vector in Escherichia coli BL21 Synechococcus elongatus PCC 7942 = FACHB-805

Inhibitors

Inhibitors Comment Organism Structure
additional information product inhibition through interaction with either the protease or the parent protein. The former leads to cleavage of the daughter proteins and can account for reduced cleavage of parent photolyase Synechococcus elongatus PCC 7942 = FACHB-805

Organism

Organism UniProt Comment Textmining
Synechococcus elongatus PCC 7942 = FACHB-805
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Purification (Commentary)

Purification (Comment) Organism
by gel filtration Synechococcus elongatus PCC 7942 = FACHB-805

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information with photolyase (PL), proteinase K (PK) generates two large daughter proteins (PL-PK1 and PL-PK2), and lower molecular products (PL-PK3 and PL-PK4). PL-PK3 and PL-PK4 may derive from secondary proteolysis of PL-PK1 and PL-PK2, respectively. In photolyase, proteinase K is active at both proteolysis sites. Cleavage to yield PL-chymotrypsin, and PL-PK1 occurs at a common site in photolyase, specifically within the N-terminal, alpha/beta-domain at the W98-N99 and E94-A95 peptide bonds, respectively. PL-PK2 is generated by a cleavage between residues 402 and 404 Synechococcus elongatus PCC 7942 = FACHB-805 ?
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