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

BRENDA support

Literature summary for 2.7.7.42 extracted from

  • Nolden, L.; Farwick, M.; Krไmer, R.; Burkovski, A.
    Glutamine synthetases of Corynebacterium glutamicum: transcriptional control and regulation of activity (2001), FEBS Lett., 201, 91-98.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of null mutant LNDELTAglnE strain with chromosomal deletion of gene glnE, the mutant does not respond to nitrogen level like the wild-type, the mutant shows a higher [L-glutamate:ammonia ligase (ADP-forming)] activity level compared to the wild-type when grown in nitrogen-rich medium due to upregulation of glnA Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [L-glutamate:ammonia ligase (ADP-forming)] Corynebacterium glutamicum enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q79VE2 strains ATCC 13032 and null mutant LNDELTAglnE
-
Corynebacterium glutamicum Q79VE2 gene glnE in one operon with gene glnA2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
Corynebacterium glutamicum diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)] enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity Corynebacterium glutamicum diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
?