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Literature summary for 5.4.3.8 extracted from

  • Campanini, B.; Bettati, S.; di Salvo, M.L.; Mozzarelli, A.; Contestabile, R.
    Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution (2013), BioMed Res. Int., 2013, 353270.
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate 1-semialdehyde Synechococcus sp.
-
 5-aminolevulinate
-
 ?

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-glutamate 1-semialdehyde = 5-aminolevulinate catalytic mechanism via external aldimine and Gem-diamine intermediates, overview Synechococcus sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate 1-semialdehyde
-
 Synechococcus sp. 5-aminolevulinate
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Synechococcus sp.

Synonyms

Synonyms Comment Organism
glutamate-1-semialdehyde aminomutase
-
 Synechococcus sp.
GSAM
-
 Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, during the catalytic cycle, the cofactor undergoes conversion from pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate, conformational changes and binding structures, overview Synechococcus sp.

General Information

General Information Comment Organism
additional information the entrance of the catalytic site is protected by a loop that is believed to switch from an open to a closed conformation during catalysis. The structure of the mobile loop is related to the form of the cofactor bound to the active site, allowing for asymmetry within the dimer the structure of the mobile loop is related to the form of the cofactor bound to the active site, allowing for asymmetry within the dimer. Conformation of the active site loop in different crystal forms of dimeric and active site accessibility, overview Synechococcus sp.