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

BRENDA support

Literature summary for 1.4.1.2 extracted from

  • Paradisi, F.; Woolfson, R.; Geoghegan, K.F.; Engel, P.C.
    Identification of the residue responsible for catalysing regeneration of activity in the inactive glutamate dehydrogenase mutant D165N (2005), FEBS Lett., 579, 2830-2832.
    View publication on PubMed

Application

Application Comment Organism
additional information reactivation of D165N is a consequence of the catalytic chemistry of the enzyme’s active site [Clostridium] symbiosum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli TG1 [Clostridium] symbiosum

Protein Variants

Protein Variants Comment Organism
D165N/K125A correctly folded, no significant deamidation [Clostridium] symbiosum

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate)
-
[Clostridium] symbiosum

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration [Clostridium] symbiosum

Synonyms

Synonyms Comment Organism
glutamate dehydrogenase
-
[Clostridium] symbiosum

Cofactor

Cofactor Comment Organism Structure
NAD+ protects against targeting the Cys320 in the active site by 5,5'-dithiobis(2-nitrobenzoate) [Clostridium] symbiosum