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Literature summary for 1.3.7.4 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)

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

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Superdex 200 gel filtration Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
HY2
-
Arabidopsis thaliana
phytochromobilin synthase
-
Arabidopsis thaliana
PphiB synthase
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
Ferredoxin dependent Arabidopsis thaliana