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

BRENDA support

Literature summary for 3.2.2.24 extracted from

  • Kim, K.; Zhang, Y.; Roberts, G.P.
    Characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum (2004), FEBS Lett., 559, 84-88.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C102S enzyme maintains activity after removal of light, shows a significantly poorer affinity for Mn2+, and higher affinity for the calcium site of the hydroxylapatite column than wild-type Rhodospirillum rubrum
N100K enzyme maintains activity after removal of light and does not respond to addition of NH4Cl, shows a significantly poorer affinity for Mn2+ and higher affinity for the calcium site of the hydroxylapatite column than wild-type Rhodospirillum rubrum
V98L enzyme maintains activity after removal of light, and shows higher affinity for the calcium site of the hydroxylapatite column than wild-type Rhodospirillum rubrum

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
-
-
-