Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tu, S.L.; Chen, H.C.; Ku, L.W.
    Mechanistic studies of the phytochromobilin synthase HY2 from Arabidopsis (2008), J. Biol. Chem., 283, 27555-27564.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.4 expressed in Escherichia coli strain BL21 Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.4 D116N mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein Arabidopsis thaliana
1.3.7.4 D146N mutant completely loses catalytic activity and also the ability of biliverdin binding Arabidopsis thaliana
1.3.7.4 D256E mutant retains only partial activity Arabidopsis thaliana
1.3.7.4 N133 mutant produces only partial activity Arabidopsis thaliana
1.3.7.4 R252Q mutant loses catalytic activity and the ability of substrate binding Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.4 Arabidopsis thaliana
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.4 Superdex 200 gel filtration Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.3.7.4 HY2
-
Arabidopsis thaliana
1.3.7.4 phytochromobilin synthase
-
Arabidopsis thaliana
1.3.7.4 PphiB synthase
-
Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.4 Ferredoxin dependent Arabidopsis thaliana